The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain

Gomis-Rüth, F.X., Gohlke, U., Betz, M., Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Murphy, G., López-Otı́n, C. and Bode, W. 1996. The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain. Journal of Molecular Biology 264 (3) , pp. 556-566. 10.1006/jmbi.1996.0661

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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 anR-value of 0.195 using data to 2.7 Å resolution. This structure reveals a disk-like shape. The chain is folded into a β-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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Elsevier
ISSN:	0022-2836
Date of Acceptance:	17 September 1996
Last Modified:	11 Sep 2023 08:44
URI:	https://orca.cardiff.ac.uk/id/eprint/161598

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