Abstract:
:The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Arendt Y,Banci L,Bertini I,Cantini F,Cozzi R,Del Conte R,Gonnelli Ldoi
10.1016/j.febslet.2007.08.069subject
Has Abstractpub_date
2007-10-02 00:00:00pages
4723-6issue
24eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00956-8journal_volume
581pub_type
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