Crystal structure of the catalytic domain of human ADAM33

J Mol Biol. 2004 Jan 2;335(1):129-37. doi: 10.1016/j.jmb.2003.10.037.

Abstract

Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • ADAM Proteins
  • Amino Acid Sequence
  • Catalytic Domain*
  • Crystallography, X-Ray*
  • Enzyme Inhibitors / chemistry
  • Humans
  • Hydroxamic Acids / chemistry
  • Metalloendopeptidases / chemistry*
  • Metalloendopeptidases / genetics
  • Models, Molecular
  • Molecular Structure
  • Mutation
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment

Substances

  • Enzyme Inhibitors
  • Hydroxamic Acids
  • marimastat
  • ADAM Proteins
  • ADAM33 protein, human
  • Metalloendopeptidases