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

Overview

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.

About this Structure

1PEX is a Single protein structure of sequence from Homo sapiens with SO4, CL and CA as ligands. Full crystallographic information is available from OCA.

Reference

The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain., Gomis-Ruth FX, Gohlke U, Betz M, Knauper V, Murphy G, Lopez-Otin C, Bode W, J Mol Biol. 1996 Dec 6;264(3):556-66. PMID:8969305

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