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Catalytic Domain of MMP20 (Enamelysin) - The NMR Structure of a New Matrix Metalloproteinase

Catalytic Domain of MMP20 (Enamelysin) - The NMR Structure of a New Matrix Metalloproteinase

Yvonne Arendt, Lucia Banci, Ivano Bertini, Francesca Cantini, Roberta Cozzi, Rebecca Del Conte, Leonardo Gonnelli

FEBS Lett. 2007 Oct 2;581(24):4723-6.

PMID: 17869250

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP161314176-B	NNGH		161314-17-6	Price

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