3ga0 | pdb_00003ga0

CtBP1/BARS Gly172->Glu mutant structure: impairing NAD(H) binding and dimerization

spinqualitylabelsall models 3ga0, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ga0 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMT Related: 1hl3, 1hku, 2hu2 Gene: Ctbp1, Bars, Ctbp3 (Rattus norvegicus) Resources: FirstGlance, OCA, RCSB, PDBsum 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 C-terminal binding proteins (CtBPs) are multi-functional proteins involved in nuclear transcriptional co-repression, Golgi membrane fission, and synaptic ribbon formation. Binding of NAD(H) to CtBPs promotes dimerization. CtBP dimers act as a scaffold for multimeric protein complex formation, thus bridging transcriptional repressors and their targets in the nucleus. Based on size-exclusion chromatography experiments and on the crystal structure of the NAD(H)-free G172E CtBP mutant, we show here that absence of NAD(H) induces flexibility/backbone conformational changes at the dimerization interface and at the CtBP interdomain region. The results presented shed first light on the correlation between NAD(H)-binding and functional CtBP dimerization. CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization.,Nardini M, Valente C, Ricagno S, Luini A, Corda D, Bolognesi M Biochem Biophys Res Commun. 2009 Mar 27;381(1):70-4. Epub 2009 Feb 10. PMID:19351597 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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