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. © 2007 Federation of European Biochemical Societies.

Catalytic domain of MMP20 (Enamelysin) - the NMR strucutre of a new matrix metalloproteinase / Y.Arendt;L.Banci;I.Bertini;F.Cantini;R.Cozzi;R.Del Conte;L.Gonnelli. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 581:(2007), pp. 4723-4726. [10.1016/j.febslet.2007.08.069]

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

BANCI, LUCIA;BERTINI, IVANO;CANTINI, FRANCESCA;DEL CONTE, REBECCA;GONNELLI, LEONARDO
2007

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. © 2007 Federation of European Biochemical Societies.
2007
581
4723
4726
Y.Arendt;L.Banci;I.Bertini;F.Cantini;R.Cozzi;R.Del Conte;L.Gonnelli
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/250747
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