| pubmed-article:17244604 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C1416502 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C0052350 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C1749428 | lld:lifeskim |
| pubmed-article:17244604 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:17244604 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:17244604 | pubmed:dateCreated | 2007-3-26 | lld:pubmed |
| pubmed-article:17244604 | pubmed:abstractText | Data relating to the structural basis of ligand recognition by integrins are limited. Here we describe the physical requirements for high affinity binding of ligands to alpha v beta6. By combining a series of structural analyses with functional testing, we show that 20-mer peptide ligands, derived from high affinity ligands of alpha v beta6 (foot-and-mouth-disease virus, latency associated peptide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed immediately by a C-terminal helix. This arrangement allows two conserved Leu/Ile residues at Asp(+1) and Asp(+4) to be presented on the outside face of the helix enabling a potential hydrophobic interaction with the alpha v beta6 integrin, in addition to the Arg-Gly-Asp interaction. The extent of the helix determines peptide affinity for alpha v beta6 and potency as an alpha v beta6 antagonist. A major role of this C-terminal helix is likely to be the correct positioning of the Asp(+1) and Asp(+4) residues. These data suggest an explanation for several biological functions of alpha v beta6 and provide a structural platform for design of alpha v beta6 antagonists. | lld:pubmed |
| pubmed-article:17244604 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17244604 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17244604 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17244604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17244604 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17244604 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17244604 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17244604 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:MarshallJohn... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:HowardMark... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:HartIan RIR | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:WeinrebPaul... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:VioletteSheli... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:SutcliffeJuli... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:DiCaraDaniell... | lld:pubmed |
| pubmed-article:17244604 | pubmed:author | pubmed-author:RapisardaChia... | lld:pubmed |
| pubmed-article:17244604 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17244604 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:17244604 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17244604 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17244604 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17244604 | pubmed:pagination | 9657-65 | lld:pubmed |
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| pubmed-article:17244604 | pubmed:meshHeading | pubmed-meshheading:17244604... | lld:pubmed |
| pubmed-article:17244604 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17244604 | pubmed:articleTitle | Structure-function analysis of Arg-Gly-Asp helix motifs in alpha v beta 6 integrin ligands. | lld:pubmed |
| pubmed-article:17244604 | pubmed:affiliation | Tumour Biology Centre, Cancer Research UK Clinical Centre, Queen Mary's College, Barts and the London Medical and Dental School, UK. | lld:pubmed |
| pubmed-article:17244604 | pubmed:publicationType | Journal Article | lld:pubmed |
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