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http://purl.uniprot.org/citations/16950398http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16950398http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16950398http://www.w3.org/2000/01/rdf-schema#comment"The SCAN domain mediates interactions between members of a subfamily of zinc-finger transcription factors and is found in more than 60 C2H2 zinc finger genes in the human genome, including the tumor suppressor gene myeloid zinc finger 1 (MZF1). Glutathione-S-transferase pull-down assays showed that the MZF1 SCAN domain self-associates, and a Kd value of 600 nM was measured by intrinsic tryptophan fluorescence polarization. The MZF1 structure determined by NMR spectroscopy revealed a domain-swapped dimer. Each monomer consists of five alpha helices in two subdomains connected by the alpha2-alpha3 loop. Residues from helix 3 of each monomer compose the core of the dimer interface, while the alpha1-alpha2 loop and helix 2 pack against helices 3 and 5 from the opposing monomer. Comprehensive sequence analysis is coupled with the first high-resolution structure of a SCAN dimer to provide an initial view of the recognition elements that govern dimerization for this large family of transcription factors."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.07.063"xsd:string
http://purl.uniprot.org/citations/16950398http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.07.063"xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Peterson F.C."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Peterson F.C."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Jensen D.R."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Jensen D.R."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Waltner J.K."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Waltner J.K."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Hayes P.L."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Hayes P.L."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Heisner A.K."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Heisner A.K."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Sander T.L."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/author"Sander T.L."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/pages"137-147"xsd:string
http://purl.uniprot.org/citations/16950398http://purl.uniprot.org/core/pages"137-147"xsd:string