1AVF

ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH

1AVF の概要

• エントリーDOI: 10.2210/pdb1avf/pdb
• 分子名称: GASTRICSIN, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: aspartyl protease, gastricsin, aspartic proteinase, intermediate, activation, acid
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P20142 P20142
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76920.20

構造登録者

Khan, A.R.,Cherney, M.M.,Tarasova, N.I.,James, M.N.G. (登録日: 1997-09-16, 公開日: 1998-02-25, 最終更新日: 2024-10-30)

主引用文献

Khan, A.R.,Cherney, M.M.,Tarasova, N.I.,James, M.N.
Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin.
Nat.Struct.Biol., 4:1010-1015, 1997

PubMed Abstract: The crystal structure of an activation intermediate of human gastricsin has been determined at 2.4 A resolution. The human digestive enzyme gastricsin (pepsin C) is an aspartic proteinase that is synthesized as the inactive precursor (zymogen) progastricsin (pepsinogen C or hPGC). In the zymogen, a positively-charged N-terminal prosegment of 43 residues (Ala 1p-Leu 43p; the suffix 'p' refers to the prosegment) sterically prevents the approach of a substrate to the active site. Zymogen conversion occurs in an autocatalytic and stepwise fashion at low pH through the formation of intermediates. The structure of the non-covalent complex of a partially-cleaved peptide of the prosegment (Ala 1p-Phe 26p) with mature gastricsin (Ser 1-Ala 329) suggests an activation pathway that may be common to all gastric aspartic proteinases.

PubMed: 9406551
DOI: 10.1038/nsb1297-1010

実験手法

X-RAY DIFFRACTION (2.36 Å)