title: 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.
authors.affiliation: ProtEra S.r.l., Via delle Idee 22, 50019 Sesto Fiorentino (FI), Italy.
authors.forename: Yvonne
authors.initials: Y
authors.lastname: Arendt
authors.forename: Lucia
authors.initials: L
authors.lastname: Banci
authors.forename: Ivano
authors.initials: I
authors.lastname: Bertini
authors.forename: Francesca
authors.initials: F
authors.lastname: Cantini
authors.forename: Roberta
authors.initials: R
authors.lastname: Cozzi
authors.forename: Rebecca
authors.initials: R
authors.lastname: Del Conte
authors.forename: Leonardo
authors.initials: L
authors.lastname: Gonnelli
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D053519:Matrix Metalloproteinase 20 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein
chemical_list: D053519:Matrix Metalloproteinase 20