2BOA
Human procarboxypeptidase A4.
2BOA の概要
| エントリーDOI | 10.2210/pdb2boa/pdb |
| 関連するPDBエントリー | 2BO9 |
| 分子名称 | CARBOXYPEPTIDASE A4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | metalloprocarboxypeptidase, x-ray crystal structure, zymogen, metalloprotease, exopropeptidase, hydrolase, carboxypeptidase |
| 由来する生物種 | HOMO SAPIENS (HUMAN) |
| 細胞内の位置 | Secreted : Q9UI42 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 92370.65 |
| 構造登録者 | Garcia-Castellanos, R.,Bonet-Figueredo, R.,Pallares, I.,Ventura, S.,Aviles, F.X.,Vendrell, J.,Gomis-Ruth, F.X. (登録日: 2005-04-08, 公開日: 2005-12-13, 最終更新日: 2024-10-16) |
| 主引用文献 | Garcia-Castellanos, R.,Bonet-Figueredo, R.,Pallares, I.,Ventura, S.,Aviles, F.X.,Vendrell, J.,Gomis-Ruth, F.X. Detailed Molecular Comparison between the Inhibition Mode of A/B-Type Carboxypeptidases in the Zymogen State and by the Endogenous Inhibitor Latexin. Cell.Mol.Life Sci., 62:1996-, 2005 Cited by PubMed Abstract: Treatment of advanced stages of prostate carcinoma with histone-deacetylase inhibitors entails expression of human procarboxypeptidase-A4 (hPCPA4). The three-dimensional structure of hPCPA4 has been solved and shows the features of related metallocarboxypeptidase zymogens, with a preformed alpha/beta/-hydrolase active-enzyme moiety (hCPA4) and an inhibiting pro-domain (PD). The protease moiety recalls a sphere, out of which a spherical cone has been cut. This results in a funnel-like structure, at the bottom of which the active-site cleft resides. The border of this funnel is shaped by loops, which are responsible for the interaction with the PD, characterised by a large interface area and relatively few contacts. Such an inhibitory mode is evocative of the recently reported structure of the human inhibitor latexin in its complex with hCPA4. The main contacting structure of latexin is similar to the one employed for PD inhibition. In both cases, active-site blocking relies mainly on a loop provided by the central part of a beta sheet. PubMed: 16091843DOI: 10.1007/S00018-005-5174-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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