1RTG

C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2

1RTG の概要

• エントリーDOI: 10.2210/pdb1rtg/pdb
• 分子名称: HUMAN GELATINASE A, CHLORIDE ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: matrix metallo proteinase (mmp), gelatinase, metzincins, metalloprotease
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P08253
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23941.83

構造登録者

Gohlke, U.,Bode, W. (登録日: 1995-12-21, 公開日: 1996-06-10, 最終更新日: 2024-11-20)

主引用文献

Gohlke, U.,Gomis-Ruth, F.X.,Crabbe, T.,Murphy, G.,Docherty, A.J.,Bode, W.
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
FEBS Lett., 378:126-130, 1996

PubMed Abstract: In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.

PubMed: 8549817
DOI: 10.1016/0014-5793(95)01435-7

実験手法

X-RAY DIFFRACTION (2.6 Å)