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Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).

ABSTRACT: The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with similar findings on MMP-12 and MMP-9 having longer and the longest linker within the family, respectively, suggests this type of conformational freedom to be a general property of all MMPs.

SUBMITTER: Bertini I

PROVIDER: S-EPMC2676012 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature

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Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).

Bertini Ivano I Fragai Marco M Luchinat Claudio C Melikian Maxime M Mylonas Efstratios E Sarti Niko N Svergun Dmitri I DI

The Journal of biological chemistry 20090312 19

The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with simila ...[more]

PMID: 19282283

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