Publication Abstract from PubMed
Mucosal addressin cell-adhesion molecule (MAdCAM-1) is a membrane-bound leukocyte receptor regulating both the passage and retention of leukocytes in mucosal tissues. A crystal structure for the two extracellular amino-terminal domains of human MAdCAM-1 has previously been reported, confirming their expected immunoglobulin superfamily topology. In this study, a second crystal structure of this fragment is described. Although the overall structure is similar to that previously reported, one edge strand in the amino-terminal domain is instead located on the opposite sheet. This alters the arrangement and conformation of amino acids in this region that have previously been shown to be crucial for ligand binding. MAdCAM-1 is also seen to form dimers within the crystal lattice, raising the possibility that oligomerization may influence the biological role of this adhesion molecule.
A reassessment of the MAdCAM-1 structure and its role in integrin recognition.,Dando J, Wilkinson KW, Ortlepp S, King DJ, Brady RL Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):233-41. Epub 2002, Jan 24. PMID:11807247[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
