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Article: SET domain protein lysine methyltransferases: Structure, specificity and catalysis

TitleSET domain protein lysine methyltransferases: Structure, specificity and catalysis
Authors
KeywordsSpecies Index: Eukaryota
Issue Date2006
PublisherBirkhaeuser Verlag AG. The Journal's web site is located at http://link.springer.de/link/service/journals/00018/index.htm
Citation
Cellular And Molecular Life Sciences, 2006, v. 63 n. 23, p. 2755-2763 How to Cite?
AbstractSite- and state-specific lysine methylation of histones is catalyzed by a family of proteins that contain the evolutionarily conserved SET domain and plays a fundamental role in epigenetic regulation of gene activation and silencing in all eukaryotes. The recently determined three-dimensional structures of the SET domains from chromosomal proteins reveal that the core SET domain structure contains a two-domain architecture, consisting of a conserved anti-parallel β-barrel and a structurally variable insert that surround a unusual knot-like structure that comprises the enzyme active site. These structures of the SET domains, either in the free state or when bound to cofactor S-adenosyl-L-homocysteine and/or histone peptide, mimicking an enzyme/cofactor/substrate complex, further yield the structural insights into the molecular basis of the substrate specificity, methylation multiplicity and the catalytic mechanism of histone lysine methylation. © Birkhäuser Verlag, 2006.
Persistent Identifierhttp://hdl.handle.net/10722/91178
ISSN
2015 Impact Factor: 5.694
2015 SCImago Journal Rankings: 3.388
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorZhou, MMen_HK
dc.date.accessioned2010-09-17T10:14:16Z-
dc.date.available2010-09-17T10:14:16Z-
dc.date.issued2006en_HK
dc.identifier.citationCellular And Molecular Life Sciences, 2006, v. 63 n. 23, p. 2755-2763en_HK
dc.identifier.issn1420-682Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/91178-
dc.description.abstractSite- and state-specific lysine methylation of histones is catalyzed by a family of proteins that contain the evolutionarily conserved SET domain and plays a fundamental role in epigenetic regulation of gene activation and silencing in all eukaryotes. The recently determined three-dimensional structures of the SET domains from chromosomal proteins reveal that the core SET domain structure contains a two-domain architecture, consisting of a conserved anti-parallel β-barrel and a structurally variable insert that surround a unusual knot-like structure that comprises the enzyme active site. These structures of the SET domains, either in the free state or when bound to cofactor S-adenosyl-L-homocysteine and/or histone peptide, mimicking an enzyme/cofactor/substrate complex, further yield the structural insights into the molecular basis of the substrate specificity, methylation multiplicity and the catalytic mechanism of histone lysine methylation. © Birkhäuser Verlag, 2006.en_HK
dc.languageengen_HK
dc.publisherBirkhaeuser Verlag AG. The Journal's web site is located at http://link.springer.de/link/service/journals/00018/index.htmen_HK
dc.relation.ispartofCellular and Molecular Life Sciencesen_HK
dc.subjectSpecies Index: Eukaryotaen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshBinding Sitesen_HK
dc.subject.meshCatalysisen_HK
dc.subject.meshHistone-Lysine N-Methyltransferase - chemistry - metabolismen_HK
dc.subject.meshHistones - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMethylationen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Conformationen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshS-Adenosylhomocysteine - metabolismen_HK
dc.subject.meshSequence Alignmenten_HK
dc.subject.meshSubstrate Specificityen_HK
dc.titleSET domain protein lysine methyltransferases: Structure, specificity and catalysisen_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s00018-006-6274-5en_HK
dc.identifier.pmid17013555en_HK
dc.identifier.scopuseid_2-s2.0-33845487512en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845487512&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume63en_HK
dc.identifier.issue23en_HK
dc.identifier.spage2755en_HK
dc.identifier.epage2763en_HK
dc.identifier.eissn1569-1632-
dc.identifier.isiWOS:000242813800006-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridZhou, MM=7403506618en_HK
dc.identifier.citeulike1034041-

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