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The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions.

Abstract:

Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP, a crystal structure of the Hpx domain was solved at 1.7 Å resolution. Two interactions were identified as potential biological dimer interfaces in the crystal structure, and mutagenesis studies revealed that the biological dimer possesses a symm...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m110.178434

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Journal:
Journal of biological chemistry
Volume:
286
Issue:
9
Pages:
7587-7600
Publication date:
2011-03-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
224444

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