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Zn-CysHis Protein Factor Families: Role of Electrostatic Interaction of Zn-Domains in Factor Functions

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dc.contributor.authorChirgadze, Y. N.
dc.contributor.authorIvanov, V. V.
dc.contributor.authorИванов, Виктор Владимирович
dc.date.accessioned2024-11-26T13:01:42Z
dc.date.available2024-11-26T13:01:42Z
dc.date.issued2020
dc.description.abstractThe large amount of the DNA- and RNA-binding protein regulatory factors contain Zn-domains. Total six Zn-CysHis factor families with different functions were considered. Among them the transcription factors of family PF00096, complex type Zn-Cys2His2, is the most important because it includes over 340.000 members of 365.000 total members listed at present in the Zn-containing factor families. The role of electrostatic potential of Zn-domains in the structure and function of factors from different factor families has been considered. We have shown that the positive electrostatic potential of Zn-domains plays an essential role in forming contact of factors' Zn-domains with DNA/RNA in three protein factor families PF00096, PF12874, and PF09329. While in other three families PF03119, PF08996, and PF01258 Zn-domains do not contact with nucleic acids, and electrostatic interactions do not play a distinctive role, consequently.
dc.format.extentС. 179-186
dc.identifier.citationChirgadze, Y. N. Zn-CysHis Protein Factor Families: Role of Electrostatic Interaction of Zn-Domains in Factor Functions / Chirgadze, Y.N., Ivanov, V.V. // Molekuliarnaia biologiia. - 2020. - 54. - № 2. - P. 179-186. - 10.31857/S0026898420020032
dc.identifier.doi10.31857/S0026898420020032
dc.identifier.urihttps://www.doi.org/10.31857/S0026898420020032
dc.identifier.urihttps://www.scopus.com/record/display.uri?eid=2-s2.0-85084607306&origin=resultslist
dc.identifier.urihttps://openrepository.mephi.ru/handle/123456789/21691
dc.relation.ispartofMolekuliarnaia biologiia
dc.titleZn-CysHis Protein Factor Families: Role of Electrostatic Interaction of Zn-Domains in Factor Functions
dc.typeArticle
dspace.entity.typePublication
oaire.citation.issue2
oaire.citation.volume54
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relation.isAuthorOfPublication.latestForDiscovery4cdac2e9-b8fc-4654-8776-529e873dad80
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