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dc.contributor.authorLiang, Yu
dc.contributor.authorHuimei Hong, Felicia
dc.contributor.authorGanesan, Pugalenthi
dc.contributor.authorJiang, Sizun
dc.contributor.authorJauch, Ralf
dc.contributor.authorStanton, Lawrence W.
dc.contributor.authorKolatkar, Prasanna R.
dc.date.accessioned2014-11-11T14:27:05Z
dc.date.available2014-11-11T14:27:05Z
dc.date.issued2012-06-25
dc.identifier.citationLiang Y, Huimei Hong F, Ganesan P, Jiang S, Jauch R, et al. (2012) Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206. Nucleic Acids Research 40: 8721-8732. doi:10.1093/nar/gks611.
dc.identifier.issn03051048
dc.identifier.pmid22735705
dc.identifier.doi10.1093/nar/gks611
dc.identifier.urihttp://hdl.handle.net/10754/334484
dc.description.abstractZfp206 (also named as Zscan10) belongs to the subfamily of C2H2 zinc finger transcription factors, which is characterized by the N-terminal SCAN domain. The SCAN domain mediates self-association and association between the members of SCAN family transcription factors, but the structural basis and selectivity determinants for complex formation is unknown. Zfp206 is important for maintaining the pluripotency of embryonic stem cells presumably by combinatorial assembly of itself or other SCAN family members on enhancer regions. To gain insights into the folding topology and selectivity determinants for SCAN dimerization, we solved the 1.85 crystal structure of the SCAN domain of Zfp206. In vitro binding studies using a panel of 20 SCAN proteins indicate that the SCAN domain Zfp206 can selectively associate with other members of SCAN family transcription factors. Deletion mutations showed that the N-terminal helix 1 is critical for heterodimerization. Double mutations and multiple mutations based on the Zfp206SCAN-Zfp110SCAN model suggested that domain swapped topology is a possible preference for Zfp206SCAN-Zfp110SCAN heterodimer. Together, we demonstrate that the Zfp206SCAN constitutes a protein module that enables C2H2 transcription factor dimerization in a highly selective manner using a domain-swapped interface architecture and identify novel partners for Zfp206 during embryonal development. 2012 The Author(s).
dc.language.isoen
dc.publisherOxford University Press (OUP)
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0
dc.subjectprotein Zfp206
dc.subjecttranscription factor
dc.subjectunclassified drug
dc.subjectamino terminal sequence
dc.subjectarticle
dc.subjectcomplex formation
dc.subjectcontrolled study
dc.subjectcrystal structure
dc.subjectdimerization
dc.subjectembryonic stem cell
dc.subjectenhancer region
dc.subjectgene deletion
dc.subjectgene mutation
dc.subjectimmunoprecipitation
dc.subjectin vitro study
dc.subjectmolecular biology
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein analysis
dc.subjectprotein binding
dc.subjectprotein domain
dc.subjectprotein expression
dc.subjectprotein family
dc.subjectprotein folding
dc.subjectprotein purification
dc.subjectprotein structure
dc.subjectSCAN domain
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCrystallography, X-Ray
dc.subjectDimerization
dc.subjectEmbryonic Stem Cells
dc.subjectMice
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.subjectSequence Alignment
dc.subjectTranscription Factors
dc.titleStructural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206
dc.typeArticle
dc.contributor.departmentBioscience Core Lab
dc.identifier.journalNucleic Acids Research
dc.identifier.pmcidPMC3458555
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionLaboratory for Structural Biochemistry, Genome Institute of Singapore, Genome, 60 Biopolis Street, Singapore 138672, Singapore
dc.contributor.institutionStem Cell and Developmental Biology, Genome Institute of Singapore, Genome, 60 Biopolis Street, Singapore 138672, Singapore
dc.contributor.institutionDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore
dc.contributor.institutionNUS Graduate School for Integrative Sciences and Engineering (NGS), Centre for Life Sciences (CeLS), #05-01, 28 Medical Drive, Singapore 117456, Singapore
dc.contributor.institutionMedicinal Chemistry Department, H073 Health Science Building, Seattle, WA 98195, United States
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personGanesan, Pugalenthi
refterms.dateFOA2018-06-13T15:33:07Z
dc.date.published-online2012-06-25
dc.date.published-print2012-09


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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.