TY  - JOUR
AU  - Bertini, I.
AU  - Fragai, M.
AU  - Luchinat, C.
AU  - Melikian, M.
AU  - Mylonas, E.
AU  - Sarti, N.
AU  - Svergun, D. I.
AU  - DESY
TI  - Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)
JO  - The journal of biological chemistry
VL  - 284
SN  - 0021-9258
CY  - Bethesda, Md.
PB  - Soc.
M1  - PHPPUBDB-11922
SP  - 12821-12828
PY  - 2009
AB  - 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.
KW  - Catalysis
KW  - Crystallography, X-Ray
KW  - Heme
KW  - Humans
KW  - Matrix Metalloproteinase 1: chemistry
KW  - Matrix Metalloproteinase 1: metabolism
KW  - Matrix Metalloproteinase 12: chemistry
KW  - Matrix Metalloproteinase 9: chemistry
KW  - Models, Molecular
KW  - Nuclear Magnetic Resonance, Biomolecular
KW  - Pliability
KW  - Protein Conformation
KW  - Protein Structure, Tertiary
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: metabolism
KW  - Recombinant Proteins (NLM Chemicals)
KW  - Heme (NLM Chemicals)
KW  - Matrix Metalloproteinase 9 (NLM Chemicals)
KW  - Matrix Metalloproteinase 12 (NLM Chemicals)
KW  - Matrix Metalloproteinase 1 (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:19282283
C2  - pmc:PMC2676012
UR  - <Go to ISI:>//WOS:000265688300027
DO  - DOI:10.1074/jbc.M809627200
UR  - https://bib-pubdb1.desy.de/record/94201
ER  -