| pubmed-article:7531291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7531291 | lifeskim:mentions | umls-concept:C0078056 | lld:lifeskim |
| pubmed-article:7531291 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:7531291 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:7531291 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:7531291 | pubmed:issue | 6514 | lld:pubmed |
| pubmed-article:7531291 | pubmed:dateCreated | 1995-3-3 | lld:pubmed |
| pubmed-article:7531291 | 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. | lld:pubmed |
| pubmed-article:7531291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7531291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7531291 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7531291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7531291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7531291 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7531291 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:HarlosKK | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:EdwardsR MRM | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:RobinsonR CRC | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:StuartD IDI | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:JonesE YEY | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:DriscollP CPC | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:ClementsJ MJM | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:DudgeonT JTJ | lld:pubmed |
| pubmed-article:7531291 | pubmed:author | pubmed-author:BottomleyM... | lld:pubmed |
| pubmed-article:7531291 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7531291 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:7531291 | pubmed:volume | 373 | lld:pubmed |
| pubmed-article:7531291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7531291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7531291 | pubmed:pagination | 539-44 | lld:pubmed |
| pubmed-article:7531291 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7531291 | pubmed:meshHeading | pubmed-meshheading:7531291-... | lld:pubmed |
| pubmed-article:7531291 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7531291 | pubmed:articleTitle | Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution. | lld:pubmed |
| pubmed-article:7531291 | pubmed:affiliation | Laboratory of Molecular Biophysics, Oxford Centre for Molecular Sciences, UK. | lld:pubmed |
| pubmed-article:7531291 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7531291 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:7412 | entrezgene:pubmed | pubmed-article:7531291 | lld:entrezgene |
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