Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6514
|
pubmed:dateCreated |
1995-3-3
|
pubmed:abstractText |
The cell-surface glycoprotein vascular cell adhesion molecule-1 (VCAM-1; ref. 1) mediates intercellular adhesion by specific binding to the integrin very-late antigen-4 (VLA-4, alpha 4 beta 1; ref. 3). VCAM-1, with the intercellular adhesion molecules ICAM-1, ICAM-2, ICAM-3 and the mucosal vascular addressin MAd-CAM-1, forms an integrin-binding subgroup of the immunoglobulin superfamily. In addition to their clinical relevance in inflammation, these molecules act as cellular receptors for viral and parasitic agents. The predominant form of VCAM-1 in vivo has an amino-terminal extracellular region comprising seven immunoglobulin-like domains. Functional studies have identified a conserved integrin-binding motif in domains 1 and 4, variants of which are present in the N-terminal domain of all members of the immunoglobulin superfamily subgroup. We report here the crystal structure of a VLA-4-binding fragment composed of the first two domains of VCAM-1. The integrin-binding motif (Q38IDSPL) is highly exposed and forms the N-terminal region of the loop between beta-strands C and D of domain 1. This motif exhibits a distinctive conformation which we predict will be common to all the integrin-binding IgSF molecules. These, and additional data, map VLA-4 binding to the face of the CFG beta-sheet, the surface previously identified as the site for intercellular adhesive interactions between members of the immunoglobulin superfamily.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD2,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Very Late Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0028-0836
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
9
|
pubmed:volume |
373
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
539-44
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7531291-Amino Acid Sequence,
pubmed-meshheading:7531291-Antigens, CD2,
pubmed-meshheading:7531291-Binding Sites,
pubmed-meshheading:7531291-Cell Adhesion Molecules,
pubmed-meshheading:7531291-Computer Graphics,
pubmed-meshheading:7531291-Crystallography, X-Ray,
pubmed-meshheading:7531291-Escherichia coli,
pubmed-meshheading:7531291-Humans,
pubmed-meshheading:7531291-Molecular Sequence Data,
pubmed-meshheading:7531291-Mutagenesis,
pubmed-meshheading:7531291-Protein Conformation,
pubmed-meshheading:7531291-Protein Structure, Secondary,
pubmed-meshheading:7531291-Receptors, Very Late Antigen,
pubmed-meshheading:7531291-Recombinant Proteins,
pubmed-meshheading:7531291-Sequence Homology, Amino Acid,
pubmed-meshheading:7531291-Vascular Cell Adhesion Molecule-1
|
pubmed:year |
1995
|
pubmed:articleTitle |
Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution.
|
pubmed:affiliation |
Laboratory of Molecular Biophysics, Oxford Centre for Molecular Sciences, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|