| http://purl.uniprot.org/citations/7594538 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7594538 | http://www.w3.org/2000/01/rdf-schema#comment | "The integrin receptors alpha 4 beta 1 and alpha 4 beta 7 both bind to vascular cell adhesion molecule-1 (VCAM-1). Here, we report that the amino acid residue requirements for murine VCAM-1 adhesion to murine alpha 4 beta 1 (WEHI 231) and alpha 4 beta 7 (38C13/beta 7-transfectant) positive cells are strikingly similar but nonidentical under multiple adhesion activity states. By site-directed mutagenesis of domain 1 of VCAM-1, the amino acid residues on the loop between beta strands C and D (R36, Q38, I39, D40, P42) and on the adjacent antiparallel beta strand F (L70 and T72) were required for basal level adhesion to both alpha 4 beta 1-positive and alpha 4 beta 7-positive cells. Mutation at two other sites, N44 (loop between beta strands C and D) and E66 (loop between beta strands E and F), specifically reduced alpha 4 beta 7-positive cell adhesion, but not alpha 4 beta 1-positive cell adhesion. Mutation H85A augmented alpha 4 beta 7 binding but not alpha 4 beta 1 binding. These apparent differences relate to the higher intrinsic activity state of alpha 4 beta 1 on WEHI 231 than on alpha 4 beta 7 (38C13/beta 7-transfectant). In contrast, under higher adhesion activity states induced by either MnCl2 or truncation of the beta 7 cytoplasmic tail, mutation of either amino acid residue D40 or L70 completely blocked cell adhesion without evidence of structural perturbation of VCAM-1. These results suggested that the two structurally discontinuous amino acid residues, the negatively charged D40 and the hydrophobic L70 adjacently located on domain 1 of VCAM-1, are essential for interaction under multiple activity states with both alpha 4 beta 1 and alpha 4 beta 7 integrin receptors."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Jones S."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Weissman I.L."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Fong S."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Presta L.G."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Crowe D.T."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Chiu H.H."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/author | "Renz M.E."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/pages | "5257-5267"xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/title | "Similar but nonidentical amino acid residues on vascular cell adhesion molecule-1 are involved in the interaction with alpha 4 beta 1 and alpha 4 beta 7 under different activity states."xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://purl.uniprot.org/core/volume | "155"xsd:string |
| http://purl.uniprot.org/citations/7594538 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7594538 |
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