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Crystal structure of the catalytic domain of human ADAM33.

Authors
  • Orth, Peter
  • Reichert, Paul
  • Wang, Wenyan
  • Prosise, Winifred W
  • Yarosh-Tomaine, Taisa
  • Hammond, Gerald
  • Ingram, Richard N
  • Xiao, Li
  • Mirza, Urooj A
  • Zou, Jun
  • Strickland, Corey
  • Taremi, S Shane
  • Le, Hung V
  • Madison, Vincent
Type
Published Article
Journal
Journal of molecular biology
Publication Date
Jan 02, 2004
Volume
335
Issue
1
Pages
129–137
Identifiers
PMID: 14659745
Source
Medline
License
Unknown

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.

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