3ga0
CtBP1/BARS Gly172->Glu mutant structure: impairing NAD(H) binding and dimerization
Structural highlights
FunctionCTBP1_RAT Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation.[1] [2] [3] 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 PubMedC-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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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