Journal Article

PHPPUBDB-11922

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)

Bertini, I. ; Fragai, M. ; Luchinat, C. ; Melikian, M. ; Mylonas, E. ; Sarti, N. ; Svergun, D. I. ; DESY

2009
Soc. Bethesda, Md.

This record in other databases:      

Please use a persistent id in citations: doi:10.1074/jbc.M809627200

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.

Keyword(s): Catalysis (MeSH) ; Crystallography, X-Ray (MeSH) ; Heme (MeSH) ; Humans (MeSH) ; Matrix Metalloproteinase 1: chemistry (MeSH) ; Matrix Metalloproteinase 1: metabolism (MeSH) ; Matrix Metalloproteinase 12: chemistry (MeSH) ; Matrix Metalloproteinase 9: chemistry (MeSH) ; Models, Molecular (MeSH) ; Nuclear Magnetic Resonance, Biomolecular (MeSH) ; Pliability (MeSH) ; Protein Conformation (MeSH) ; Protein Structure, Tertiary (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: metabolism (MeSH) ; Recombinant Proteins ; Heme ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinase 12 ; Matrix Metalloproteinase 1

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Contributing Institute(s):

1. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2009
Notes: (c) 2010 by American Society for Biochemistry and Molecular Biology. No copyright permission for full text.

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Database coverage:
; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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