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• W2003406962 abstract "The osteopontin SVVYGLR motif binds the integrins alpha(4)beta(1) and alpha(9)beta(1). We show that alpha(4)beta(7) also interacts with this motif and that an SVVYGLR-OH peptide antagonises the alpha(4)beta(7) MAdCAM interaction. The important elements of this motif required to bind alpha(4)beta(1) and alpha(4)beta(7) were probed using a series of mutated peptides based around SVVYGLR. Leu167 is important for the interaction with alpha(4) integrins, as is the C-terminal carboxylic acid of Arg168 exposed by thrombin cleavage. The importance of the acidic group means that SVVYGLR has structural elements in common with other alpha(4) integrin-binding motifs and suggests why thrombin cleavage activates this motif." @default.
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• W2003406962 date "2001-08-10" @default.
• W2003406962 modified "2023-10-17" @default.
• W2003406962 title "Structural elements of the osteopontin SVVYGLR motif important for the interaction with α₄ integrins" @default.
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• W2003406962 doi "https://doi.org/10.1016/s0014-5793(01)02690-4" @default.
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