1gsm

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(New page: 200px<br /><applet load="1gsm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsm, resolution 1.90&Aring;" /> '''A REASSESSMENT OF TH...)
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Revision as of 14:08, 20 November 2007


1gsm, resolution 1.90Å

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A REASSESSMENT OF THE MADCAM-1 STRUCTURE AND ITS ROLE IN INTEGRIN RECOGNITION.

Overview

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.

About this Structure

1GSM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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