Send to

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):233-41. Epub 2002 Jan 24.

A reassessment of the MAdCAM-1 structure and its role in integrin recognition.

Author information

  • 1Department of Biochemistry, University of Bristol, Bristol BS8 1TD, England.


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.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for International Union of Crystallography
    Loading ...
    Support Center