2kr1 | pdb_00002kr1

Solution NMR structure of zinc binding N-terminal domain of ubiquitin-protein ligase E3A from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HR3662

spinqualitylabelsall models 2kr1, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kr1 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Gene: UBE3A, hCG_18679 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling degradation of p53. This article describe the solution NMR structure of the conserved N-terminal domain of human Ube3A (residues 24-87) that contains two residues (Cys44 and Arg62) found to be mutated in patients with Angelman syndrome. The structure of this domain adopts a novel Zn-binding fold we called AZUL (Amino-terminal Zn-finger of Ube3a Ligase). The AZUL domain has a helix-loop-helix architecture with a Zn ion coordinated by four Cys residues arranged in Cys-X(4)-Cys-X(4)-Cys-X(28)-Cys motif. Three of the Zn-bound residues are located in a 23-residue long and well structured loop that connects two alpha-helicies. Zn-binding AZUL domain of human ubiquitin protein ligase Ube3A.,Lemak A, Yee A, Bezsonova I, Dhe-Paganon S, Arrowsmith CH J Biomol NMR. 2011 Sep;51(1-2):185-90. Epub 2011 Sep 27. PMID:21947926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin protein ligase

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