2jsd
From Proteopedia
Solution structure of MMP20 complexed with NNGH
Structural highlights
DiseaseMMP20_HUMAN Defects in MMP20 are the cause of amelogenesis imperfecta hypomaturation type 2A2 (AI2A2) [MIM:612529. AI2A2 is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.[1] FunctionMMP20_HUMAN Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation.[2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.,Arendt Y, Banci L, Bertini I, Cantini F, Cozzi R, Del Conte R, Gonnelli L FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6. PMID:17869250[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Arendt Y | Banci L | Bertini I | Cantini F | Cozzi R | Del Conte R | Gonnelli L
