1CGH

Human cathepsin G

1CGH の概要

• エントリーDOI: 10.2210/pdb1cgh/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000399
• 分子名称: CATHEPSIN G, N-(3-carboxypropanoyl)-L-valyl-N-{(1R)-1-[(S)-hydroxy(oxido)phosphanyl]-2-phenylethyl}-L-prolinamide (3 entities in total)
• 機能のキーワード: inflammation, specificity, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell surface: P08311
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25981.69

構造登録者

Hof, P.,Bode, W. (登録日: 1996-06-26, 公開日: 1997-07-07, 最終更新日: 2024-10-30)

主引用文献

Hof, P.,Mayr, I.,Huber, R.,Korzus, E.,Potempa, J.,Travis, J.,Powers, J.C.,Bode, W.
The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities.
EMBO J., 15:5481-5491, 1996

PubMed Abstract: The crystal structure of human neutrophil cathepsin G, complexed with the peptidyl phosphonate inhibitor Suc-Val-Pro-PheP-(OPh)2, has been determined to a resolution of 1.8 A using Patterson search techniques. The cathepsin G structure shows the polypeptide fold characteristic of trypsin-like serine proteinases and is especially similar to rat mast cell proteinase II. Unique to cathepsin G, however, is the presence of Glu226 (chymotrypsinogen numbering), which is situated at the bottom of the S1 specificity pocket, dividing it into two compartments. For this reason, the benzyl side chain of the inhibitor PheP residue does not fully occupy the pocket but is, instead, located at its entrance. Its positively charged equatorial edge is involved in a favourable electrostatic interaction with the negatively charged carboxylate group of Glu226. Arrangement of this Glu226 carboxylate would also allow accommodation of a Lys side chain in this S1 pocket, in agreement with the recently observed cathepsin G preference for Lys and Phe at P1. The cathepsin G complex with the covalently bound phosphonate inhibitor mimics a tetrahedral substrate intermediate. A comparison of the Arg surface distributions of cathepsin G, leukocyte elastase and rat mast cell protease II shows no simple common recognition pattern for a mannose-6-phosphate receptor-independent targeting mechanism for sorting of these granular proteinases.

PubMed: 8896442

実験手法

X-RAY DIFFRACTION (1.8 Å)