1e0l
From Proteopedia
FBP28WW domain from Mus musculus
Structural highlights
FunctionTCRG1_MOUSE Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence. Structural analysis of WW domains and design of a WW prototype.,Macias MJ, Gervais V, Civera C, Oschkinat H Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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