4a94

Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4

spinqualitylabelsall models 4a94, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a94 is a 4 chain structure with sequence from Four-tooth nerite and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NO3, ZN Related: 2boa, 2bo9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CBPA4_HUMAN] Metalloprotease that could be involved in the histone hyperacetylation pathway. Publication Abstract from PubMed NvCI is a novel exogenous proteinaceous inhibitor of metallo-carboxypeptidases from the marine snail Nerita versicolor. The complex between human carboxypeptidase 4 (hCPA4) and NvCI has been crystallized and determined at 1.7 A resolution. The NvCI structure defines a distinctive protein fold basically composed by a two-stranded antiparallel beta-sheet connected by three loops, the inhibitory C-terminal tail and stabilized by three disulphide bridges. NvCI is a tight-binding inhibitor that interacts with the active site of the enzyme in a substrate-like manner. NvCI displays an extended and novel interface with hCPA4, responsible of inhibitory constant values in the picomolar range for some members of the M14A subfamily of carboxypeptidases. This makes NvCI the strongest inhibitor reported so far for this family. The structural homology displayed by the C-terminal tails of different carboxypeptidase inhibitors represents a relevant example of convergent evolution. Crystal structure of a novel metallo-carboxypeptidase inhibitor from the marine mollusk Nerita versicolor in complex with human carboxypeptidase A4.,Covaleda G, Alonso Del Rivero M, Chavez MA, Aviles FX, Reverter D J Biol Chem. 2012 Jan 31. PMID:22294694 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carboxypeptidase

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