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

被引:60
作者
Bertini, Ivano [1 ,2 ]
Fragai, Marco [1 ,3 ]
Luchinat, Claudio [1 ,3 ]
Melikian, Maxime [1 ]
Mylonas, Efstratios [4 ]
Sarti, Niko [1 ,2 ]
Svergun, Dmitri I. [4 ,5 ]
机构
[1] Univ Florence, Magnet Resonance Ctr, I-50019 Sesto Fiorentino, Italy
[2] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy
[3] Univ Florence, Dept Agr Biotechnol, I-50144 Florence, Italy
[4] Hamburg Outstn, European Mol Biol Lab, D-22603 Hamburg, Germany
[5] Russian Acad Sci, Inst Crystallog, Moscow 117333, Russia
关键词
C-TERMINAL DOMAIN; NEUTROPHIL COLLAGENASE; CRYSTAL-STRUCTURE; CATALYTIC DOMAIN; SUBSTRATE-SPECIFICITY; SURFACE ACCESSIBILITY; ACTIVATION MECHANISM; TISSUE INHIBITORS; PEPTIDE MODELS; NMR RELAXATION;
D O I
10.1074/jbc.M809627200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of fulllength 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.
引用
收藏
页码:12821 / 12828
页数:8
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