2jyd

Structure of the fifth zinc finger of Myelin Transcription Factor 1

spinqualitylabelsall models 2jyd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jyd is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYT1_MOUSE Binds to the promoter regions of proteolipid proteins of the central nervous system. May play a role in the development of neurons and oligodendrogalia in the CNS. May regulate a critical transition point in oligodendrocyte lineage development by modulating oligodendrocyte progenitor proliferation relative to terminal differentiation and up-regulation of myelin gene transcription (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 PubMed Zinc binding domains, or zinc fingers (ZnFs), form one of the most numerous and most diverse superclasses of protein structural motifs in eukaryotes. Although our understanding of the functions of several classes of these domains is relatively well developed, we know much less about the molecular mechanisms of action of many others. Myelin transcription factor 1 (MyT1) type ZnFs are found in organisms as diverse as nematodes and mammals and are found in a range of sequence contexts. MyT1, one of the early transcription factors expressed in the developing central nervous system, contains seven MyT1 ZnFs that are very highly conserved both within the protein and between species. We have used a range of biophysical techniques, including NMR spectroscopy and data-driven macromolecular docking, to investigate the structural basis for the interaction between MyT1 ZnFs and DNA. Our data indicate that MyT1 ZnFs recognize the major groove of DNA in a way that appears to differ from other known zinc binding domains. Structural and biophysical analysis of the DNA binding properties of myelin transcription factor 1.,Gamsjaeger R, Swanton MK, Kobus FJ, Lehtomaki E, Lowry JA, Kwan AH, Matthews JM, Mackay JP J Biol Chem. 2008 Feb 22;283(8):5158-67. Epub 2007 Dec 11. PMID:18073212 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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