Crystal structure of the catalytic domain of human matrix metalloproteinase 10

J Mol Biol. 2004 Feb 20;336(3):707-16. doi: 10.1016/j.jmb.2003.12.033.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain
  • Crystallography, X-Ray
  • Humans
  • Matrix Metalloproteinase 10
  • Metalloendopeptidases / chemistry*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Structure, Tertiary*
  • Sequence Alignment

Substances

  • Metalloendopeptidases
  • Matrix Metalloproteinase 10

Associated data

  • PDB/1Q3A