Structural elements of the osteopontin SVVYGLR motif important for the interaction with alpha(4) integrins |
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Authors: | Green P M Ludbrook S B Miller D D Horgan C M Barry S T |
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Affiliation: | Systems Research, GlaxoSmithKline Medicines Research Centre, Stevenage, UK. |
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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. |
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