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1MX3

Crystal structure of CtBP dehydrogenase core holo form

Summary for 1MX3
Entry DOI10.2210/pdb1mx3/pdb
DescriptorC-terminal binding protein 1, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ACETIC ACID, ... (4 entities in total)
Functional Keywordsnuclear protein, phosphorylation, transcriptional corepressor, transcription repressor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q13363
Total number of polymer chains1
Total formula weight38862.95
Authors
Kumar, V.,Carlson, J.E.,Ohgi, K.E.,Edwards, T.E.,Rose, D.W.,Escalante, C.R.,Aggarwal, A.K. (deposition date: 2002-10-01, release date: 2002-12-18, Last modification date: 2024-02-14)
Primary citationKumar, V.,Carlson, J.E.,Ohgi, K.E.,Edwards, T.E.,Rose, D.W.,Escalante, C.R.,Aggarwal, A.K.
Transcription Corepressor CtBP Is an NAD+-Regulated Dehydrogenase
Mol.Cell, 10:857-869, 2002
Cited by
PubMed Abstract: Transcriptional repression is based on the selective actions of recruited corepressor complexes, including those with enzymatic activities. One well-characterized developmentally important corepressor is the C-terminal binding protein (CtBP). Although intriguingly related in sequence to D2 hydroxyacid dehydrogenases, the mechanism by which CtBP functions remains unclear. We report here biochemical and crystallographic studies which reveal that CtBP is a functional dehydrogenase. In addition, both a cofactor-dependent conformational change, with NAD(+) and NADH being equivalently effective, and the active site residues are linked to the binding of the PXDLS consensus recognition motif on repressors, such as E1A and RIP140. Together, our data suggest that CtBP is an NAD(+)-regulated component of critical complexes for specific repression events in cells.
PubMed: 12419229
DOI: 10.1016/S1097-2765(02)00650-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2025-07-09公开中

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