1RTG

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

Summary for 1RTG

• Entry DOI: 10.2210/pdb1rtg/pdb
• Descriptor: HUMAN GELATINASE A, CHLORIDE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: matrix metallo proteinase (mmp), gelatinase, metzincins, metalloprotease
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P08253
• Total number of polymer chains: 1
• Total formula weight: 23941.83

Authors

Gohlke, U.,Bode, W. (deposition date: 1995-12-21, release date: 1996-06-10, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)