title: Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
abstract: The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A resolution. The availability of this structure allowed us to critically examine the small differences existing between the catalytic domains of MMP-3 and MMP-10, which show the highest sequence identity among all MMPs. Furthermore, the binding mode of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time.
authors.affiliation: CERM, University of Florence and FiorGen Foundation, Via Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy. bertini@cerm.unifi.it
authors.forename: I
authors.initials: I
authors.lastname: Bertini
authors.forename: V
authors.initials: V
authors.lastname: Calderone
authors.forename: M
authors.initials: M
authors.lastname: Fragai
authors.forename: C
authors.initials: C
authors.lastname: Luchinat
authors.forename: S
authors.initials: S
authors.lastname: Mangani
authors.forename: B
authors.initials: B
authors.lastname: Terni
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D053506:Matrix Metalloproteinase 10; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D008666:Metalloendopeptidases; D053506:Matrix Metalloproteinase 10