Structural highlights
Function
[VCAM1_HUMAN] Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
An X-ray crystal structure of two N-terminal integrin-binding IgSF domains of human VCAM-1 is reported. This new crystal form shows an unusual and highly hydrated packing arrangement in which over 80% of the crystal is occupied by solvent. The relative orientations of the two domains adopt a new intermediate conformation. The tilt angle between the two domains is 19.4 degrees, compared with other related structures that have tilt angles ranging from 7.3 to 39.9 degrees. An analysis of the torsion angles shows that residues Ile88, Tyr89, Ser90, Pro92 and Glu96 play a major role in defining the interdomain conformations.
A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement.,Taylor P, Bilsland M, Walkinshaw MD Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1579-83. Epub 2001, Oct 25. PMID:11679722[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taylor P, Bilsland M, Walkinshaw MD. A new conformation of the integrin-binding fragment of human VCAM-1 crystallizes in a highly hydrated packing arrangement. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1579-83. Epub 2001, Oct 25. PMID:11679722
