Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity

Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich seq...
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Gespeichert in:

Autor*in:	Mykhailo Kopylov [verfasserIn] Trevia M. Jackson [verfasserIn] M. Elizabeth Stroupe [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	G-quadruplex G4 nucleoside diphosphate kinase NDPK

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 24(2019), 10, p 1988
Übergeordnetes Werk:	volume:24 ; year:2019 ; number:10, p 1988

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules24101988

Katalog-ID:	DOAJ048010979

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520			\|a Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s.
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allfields	10.3390/molecules24101988 doi (DE-627)DOAJ048010979 (DE-599)DOAJ13f49b98340644a1a25e77855b205070 DE-627 ger DE-627 rakwb eng QD241-441 Mykhailo Kopylov verfasserin aut Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry Trevia M. Jackson verfasserin aut M. Elizabeth Stroupe verfasserin aut In Molecules MDPI AG, 2003 24(2019), 10, p 1988 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:24 year:2019 number:10, p 1988 https://doi.org/10.3390/molecules24101988 kostenfrei https://doaj.org/article/13f49b98340644a1a25e77855b205070 kostenfrei https://www.mdpi.com/1420-3049/24/10/1988 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2019 10, p 1988
spelling	10.3390/molecules24101988 doi (DE-627)DOAJ048010979 (DE-599)DOAJ13f49b98340644a1a25e77855b205070 DE-627 ger DE-627 rakwb eng QD241-441 Mykhailo Kopylov verfasserin aut Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry Trevia M. Jackson verfasserin aut M. Elizabeth Stroupe verfasserin aut In Molecules MDPI AG, 2003 24(2019), 10, p 1988 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:24 year:2019 number:10, p 1988 https://doi.org/10.3390/molecules24101988 kostenfrei https://doaj.org/article/13f49b98340644a1a25e77855b205070 kostenfrei https://www.mdpi.com/1420-3049/24/10/1988 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2019 10, p 1988
allfields_unstemmed	10.3390/molecules24101988 doi (DE-627)DOAJ048010979 (DE-599)DOAJ13f49b98340644a1a25e77855b205070 DE-627 ger DE-627 rakwb eng QD241-441 Mykhailo Kopylov verfasserin aut Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry Trevia M. Jackson verfasserin aut M. Elizabeth Stroupe verfasserin aut In Molecules MDPI AG, 2003 24(2019), 10, p 1988 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:24 year:2019 number:10, p 1988 https://doi.org/10.3390/molecules24101988 kostenfrei https://doaj.org/article/13f49b98340644a1a25e77855b205070 kostenfrei https://www.mdpi.com/1420-3049/24/10/1988 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2019 10, p 1988
allfieldsGer	10.3390/molecules24101988 doi (DE-627)DOAJ048010979 (DE-599)DOAJ13f49b98340644a1a25e77855b205070 DE-627 ger DE-627 rakwb eng QD241-441 Mykhailo Kopylov verfasserin aut Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry Trevia M. Jackson verfasserin aut M. Elizabeth Stroupe verfasserin aut In Molecules MDPI AG, 2003 24(2019), 10, p 1988 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:24 year:2019 number:10, p 1988 https://doi.org/10.3390/molecules24101988 kostenfrei https://doaj.org/article/13f49b98340644a1a25e77855b205070 kostenfrei https://www.mdpi.com/1420-3049/24/10/1988 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2019 10, p 1988
allfieldsSound	10.3390/molecules24101988 doi (DE-627)DOAJ048010979 (DE-599)DOAJ13f49b98340644a1a25e77855b205070 DE-627 ger DE-627 rakwb eng QD241-441 Mykhailo Kopylov verfasserin aut Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s. G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry Trevia M. Jackson verfasserin aut M. Elizabeth Stroupe verfasserin aut In Molecules MDPI AG, 2003 24(2019), 10, p 1988 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:24 year:2019 number:10, p 1988 https://doi.org/10.3390/molecules24101988 kostenfrei https://doaj.org/article/13f49b98340644a1a25e77855b205070 kostenfrei https://www.mdpi.com/1420-3049/24/10/1988 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2019 10, p 1988
language	English
source	In Molecules 24(2019), 10, p 1988 volume:24 year:2019 number:10, p 1988
sourceStr	In Molecules 24(2019), 10, p 1988 volume:24 year:2019 number:10, p 1988
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institution	findex.gbv.de
topic_facet	G-quadruplex G4 nucleoside diphosphate kinase NDPK Organic chemistry
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container_title	Molecules
authorswithroles_txt_mv	Mykhailo Kopylov @@aut@@ Trevia M. Jackson @@aut@@ M. Elizabeth Stroupe @@aut@@
publishDateDaySort_date	2019-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Mykhailo Kopylov
spellingShingle	Mykhailo Kopylov misc QD241-441 misc G-quadruplex misc G4 misc nucleoside diphosphate kinase misc NDPK misc Organic chemistry Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
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topic_title	QD241-441 Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity G-quadruplex G4 nucleoside diphosphate kinase NDPK
topic	misc QD241-441 misc G-quadruplex misc G4 misc nucleoside diphosphate kinase misc NDPK misc Organic chemistry
topic_unstemmed	misc QD241-441 misc G-quadruplex misc G4 misc nucleoside diphosphate kinase misc NDPK misc Organic chemistry
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title	Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
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title_full	Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
author_sort	Mykhailo Kopylov
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author_browse	Mykhailo Kopylov Trevia M. Jackson M. Elizabeth Stroupe
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title_sort	bulged and canonical g-quadruplex conformations determine ndpk binding specificity
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title_auth	Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
abstract	Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s.
abstractGer	Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s.
abstract_unstemmed	Guanine-rich DNA strands can adopt tertiary structures known as G-quadruplexes (G4s) that form when Hoogsteen base-paired guanines assemble as planar stacks, stabilized by a central cation like K<sup<+</sup<. In this study, we investigated the conformational heterogeneity of a G-rich sequence from the 5′ untranslated region of the <i<Zea mays</i< <i<hexokinase4</i< gene. This sequence adopted an extensively polymorphic G-quadruplex, including non-canonical bulged G-quadruplex folds that co-existed in solution. The nature of this polymorphism depended, in part, on the incorporation of different sets of adjacent guanines into a quadruplex core, which permitted the formation of the different conformations. Additionally, we showed that the maize homolog of the human nucleoside diphosphate kinase (NDPK) NM23-H2 protein—ZmNDPK1—specifically recognizes and promotes formation of a subset of these conformations. Heteromorphic G-quadruplexes play a role in microorganisms’ ability to evade the host immune system, so we also discuss how the underlying properties that determine heterogeneity of this sequence could apply to microorganism G4s.
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container_issue	10, p 1988
title_short	Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity
url	https://doi.org/10.3390/molecules24101988 https://doaj.org/article/13f49b98340644a1a25e77855b205070 https://www.mdpi.com/1420-3049/24/10/1988 https://doaj.org/toc/1420-3049
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up_date	2024-07-03T15:25:26.146Z
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Bulged and Canonical G-Quadruplex Conformations Determine NDPK Binding Specificity

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