%0 Journal Article
%A Bertini, I.
%A Fragai, M.
%A Luchinat, C.
%A Melikian, M.
%A Mylonas, E.
%A Sarti, N.
%A Svergun, D. I.
%A DESY
%T Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)
%J The journal of biological chemistry
%V 284
%@ 0021-9258
%C Bethesda, Md.
%I Soc.
%M PHPPUBDB-11922
%P 12821-12828
%D 2009
%X 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.
%K Catalysis
%K Crystallography, X-Ray
%K Heme
%K Humans
%K Matrix Metalloproteinase 1: chemistry
%K Matrix Metalloproteinase 1: metabolism
%K Matrix Metalloproteinase 12: chemistry
%K Matrix Metalloproteinase 9: chemistry
%K Models, Molecular
%K Nuclear Magnetic Resonance, Biomolecular
%K Pliability
%K Protein Conformation
%K Protein Structure, Tertiary
%K Recombinant Proteins: chemistry
%K Recombinant Proteins: metabolism
%K Recombinant Proteins (NLM Chemicals)
%K Heme (NLM Chemicals)
%K Matrix Metalloproteinase 9 (NLM Chemicals)
%K Matrix Metalloproteinase 12 (NLM Chemicals)
%K Matrix Metalloproteinase 1 (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19282283
%2 pmc:PMC2676012
%U <Go to ISI:>//WOS:000265688300027
%R 10.1074/jbc.M809627200
%U https://bib-pubdb1.desy.de/record/94201