1CK7

GELATINASE A (FULL-LENGTH)

1CK7 の概要

• エントリーDOI: 10.2210/pdb1ck7/pdb
• NMR情報: BMRB: 5262
• 分子名称: PROTEIN (GELATINASE A), ZINC ION, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: hydrolase (metalloprotease), full-length, metalloproteinase, gelatinase a, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Secreted, extracellular space, extracellular matrix. Isoform 2: Cytoplasm: P08253
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71497.03

構造登録者

Morgunova, E.,Tuuttila, A.,Bergmann, U.,Isupov, M.,Lindqvist, Y.,Schneider, G.,Tryggvason, K. (登録日: 1999-04-28, 公開日: 1999-08-25, 最終更新日: 2024-11-13)

主引用文献

Morgunova, E.,Tuuttila, A.,Bergmann, U.,Isupov, M.,Lindqvist, Y.,Schneider, G.,Tryggvason, K.
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
Science, 284:1667-1670, 1999

PubMed Abstract: Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.

PubMed: 10356396
DOI: 10.1126/science.284.5420.1667

実験手法

X-RAY DIFFRACTION (2.8 Å)