• Title of article

    Crystal Structure of the Catalytic Domain of Human Matrix Metalloproteinase 10

  • Author/Authors

    I. BERTINI، نويسنده , , V. Calderone، نويسنده , , M. Fragai، نويسنده , , C. Luchinat، نويسنده , , S. Mangani، نويسنده , , B. Terni، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2004
  • Pages
    10
  • From page
    707
  • To page
    716
  • Abstract
    The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 Å 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.
  • Keywords
    matrix metalloproteinase , stromelysin-2 , MMP-10 , crystal structure , Inhibitor
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2004
  • Journal title
    Journal of Molecular Biology
  • Record number

    1243399