4A94

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

4A94 の概要

• エントリーDOI: 10.2210/pdb4a94/pdb
• 関連するPDBエントリー: 2BO9 2BOA
• 分子名称: CARBOXYPEPTIDASE A4, CARBOXYPEPTIDASE INHIBITOR, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, cpa4, nvci, pci, lci, hydrolase/hydrolase inhibitor
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Secreted (By similarity): Q9UI42
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82118.27

構造登録者

Covaleda, G.,Alonso, M.,Chavez, M.A.,Aviles, F.X.,Reverter, D. (登録日: 2011-11-23, 公開日: 2011-12-28, 最終更新日: 2024-11-20)

主引用文献

Covaleda, G.,Alonso Del Rivero, M.,Chavez, M.A.,Aviles, F.X.,Reverter, D.
Crystal Structure of a Novel Metallo-Carboxypeptidase Inhibitor from the Marine Mollusk Nerita Versicolor in Complex with Human Carboxypeptidase A4.
J.Biol.Chem., 287:9250-, 2012

PubMed Abstract: NvCI is a novel exogenous proteinaceous inhibitor of metallocarboxypeptidases from the marine snail Nerita versicolor. The complex between human carboxypeptidase A4 and NvCI has been crystallized and determined at 1.7 Å resolution. The NvCI structure defines a distinctive protein fold basically composed of a two-stranded antiparallel β-sheet connected by three loops and the inhibitory C-terminal tail and stabilized by three disulfide 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 human carboxypeptidase A4, responsible for inhibitory constants 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.

PubMed: 22294694
DOI: 10.1074/JBC.M111.330100

実験手法

X-RAY DIFFRACTION (1.7 Å)