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Elsevier, Journal of Biological Chemistry, 19(284), p. 12821-12828, 2009

DOI: 10.1074/jbc.m809627200

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Interdomain Flexibility in Full-length Matrix Metalloproteinase-1 (MMP-1)

Journal article published in 2009 by Ivano Bertini, Marco Fragai ORCID, Claudio Luchinat ORCID, Maxime Melikian, Efstratios Mylonas, Niko Sarti, Dmitri I. Svergun
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.