1R54

Crystal structure of the catalytic domain of human ADAM33

Summary for 1R54

• Entry DOI: 10.2210/pdb1r54/pdb
• Related: 1R55
• Descriptor: ADAM 33, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total)
• Functional Keywords: metalloprotease, asthma, adam, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: Q9BZ11
• Total number of polymer chains: 1
• Total formula weight: 24168.39

Authors

Orth, P.,Reicher, P.,Wang, W.,Prosise, W.W.,Yarosh-Tomaine, T.,Hammond, G.,Xiao, L.,Mirza, U.A.,Zou, J.,Strickland, C.,Taremi, S.S. (deposition date: 2003-10-09, release date: 2004-10-12, Last modification date: 2021-10-27)

Primary citation

Orth, P.,Reichert, P.,Wang, W.,Prosise, W.W.,Yarosh-Tomaine, T.,Hammond, G.,Xiao, L.,Mirza, U.A.,Zou, J.,Strickland, C.,Taremi, S.S.,Le, H.V.,Madison, V.
Crystal structre of the catalytic domain of human ADAM33
J.Mol.Biol., 335:129-137, 2004

PubMed 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.

PubMed: 14659745
DOI: 10.1016/j.jmb.2003.10.037

Experimental method

X-RAY DIFFRACTION (1.85 Å)