1PEX

COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN

Summary for 1PEX

• Entry DOI: 10.2210/pdb1pex/pdb
• Descriptor: COLLAGENASE-3, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: c-terminal hemopexin-like domain of matrix-metalloproteinase, metalloprotease
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (Probable): P45452
• Total number of polymer chains: 1
• Total formula weight: 24430.53

Authors

Gomis-Ruth, F.X.,Gohlke, U.,Betz, M.,Knauper, V.,Murphy, G.,Lopez-Otin, C.,Bode, W. (deposition date: 1996-05-24, release date: 1996-12-23, Last modification date: 2024-10-23)

Primary citation

Gomis-Ruth, F.X.,Gohlke, U.,Betz, M.,Knauper, V.,Murphy, G.,Lopez-Otin, C.,Bode, W.
The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain.
J.Mol.Biol., 264:556-566, 1996

PubMed Abstract: Collagenase-3 (MMP-13) is a matrix metalloproteinase involved in human breast cancer pathology and in arthritic processes. The crystal structure of its C-terminal haemopexin-like domain has been solved by molecular replacement and refined to an R-value of 0.195 using data to 2.7 A resolution. This structure reveals a disk-like shape. The chain is folded into a beta-propeller structure of pseudo 4-fold symmetry, with the four propeller blades arranged around a funnel-like tunnel. This central tunnel tube harbours four ions assigned as two calcium and two chloride ions. The C-terminal domain of collagenase-3 has a similar structure to the equivalent domain of gelatinase A and fibroblast collagenase 1; however, its detailed structure and surface charge pattern has a somewhat greater similarity to the latter, in agreement with the subgrouping of MMP-13 with the collagenase subfamily of MMPs. It is proposed that several small structural differences may act together to confer the characteristic binding and cleavage specificities of collagenases for triple-helical substrates, probably in co-operation with a fitting interdomain linker.

PubMed: 8969305
DOI: 10.1006/jmbi.1996.0661

Experimental method

X-RAY DIFFRACTION (2.7 Å)