Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.

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 Lett

journal_title

FEBS letters

authors

Arendt Y,Banci L,Bertini I,Cantini F,Cozzi R,Del Conte R,Gonnelli L

doi

10.1016/j.febslet.2007.08.069

subject

Has Abstract

pub_date

2007-10-02 00:00:00

pages

4723-6

issue

24

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(07)00956-8

journal_volume

581

pub_type

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