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.

Interdomain flexibility in full-lenght matrix metalloproteinase-1 (MMP-1) / I.Bertini; M.Fragai; C.Luchinat; M.Melikian; E.Mylonas; N.Sarti; D.Svergun. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 284:(2009), pp. 12821-12828. [10.1074/jbc.M809627200]

Interdomain flexibility in full-lenght matrix metalloproteinase-1 (MMP-1)

BERTINI, IVANO;FRAGAI, MARCO;LUCHINAT, CLAUDIO;MELIKIAN, MAXIME THIERRY OLIVIER;SARTI, NIKO;
2009

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.
2009
284
12821
12828
I.Bertini; M.Fragai; C.Luchinat; M.Melikian; E.Mylonas; N.Sarti; D.Svergun
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/368649
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