2JSD

Solution structure of MMP20 complexed with NNGH

Summary for 2JSD

• Entry DOI: 10.2210/pdb2jsd/pdb
• NMR Information: BMRB: 15361
• Descriptor: Matrix metalloproteinase-20, CALCIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: mmp-nngh, structural genomics, structural proteomics in europe, spine, spine-2, spine2-complexes, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): O60882
• Total number of polymer chains: 1
• Total formula weight: 18023.83

Authors

Arendt, Y.,Banci, L.,Bertini, I.,Cantini, F.,Cozzi, R.,Del Conte, R.,Gonnelli, L.,Structural Proteomics in Europe (SPINE) (deposition date: 2007-07-03, release date: 2007-11-20, Last modification date: 2024-05-29)

Primary citation

Arendt, Y.,Banci, L.,Bertini, I.,Cantini, F.,Cozzi, R.,Del Conte, R.,Gonnelli, L.
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
Febs Lett., 581:4723-4726, 2007

PubMed 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.

PubMed: 17869250
DOI: 10.1016/j.febslet.2007.08.069

Experimental method

SOLUTION NMR