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骨桥蛋白SVVYGLR基序中对与α(4)整合素相互作用重要的结构元件。

Structural elements of the osteopontin SVVYGLR motif important for the interaction with alpha(4) integrins.

作者信息

Green P M, Ludbrook S B, Miller D D, Horgan C M, Barry S T

机构信息

Systems Research, GlaxoSmithKline Medicines Research Centre, Stevenage, UK.

出版信息

FEBS Lett. 2001 Aug 10;503(1):75-9. doi: 10.1016/s0014-5793(01)02690-4.

DOI:10.1016/s0014-5793(01)02690-4
PMID:11513858
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.

摘要

骨桥蛋白的SVVYGLR基序可与整合素α(4)β(1)和α(9)β(1)结合。我们发现α(4)β(7)也与该基序相互作用，并且一种SVVYGLR-OH肽可拮抗α(4)β(7)与黏膜地址素细胞黏附分子（MAdCAM）的相互作用。使用一系列基于SVVYGLR的突变肽对结合α(4)β(1)和α(4)β(7)所需的该基序的重要元件进行了探究。亮氨酸167对于与α(4)整合素的相互作用很重要，凝血酶切割后暴露的精氨酸168的C末端羧酸也是如此。酸性基团的重要性意味着SVVYGLR与其他α(4)整合素结合基序具有共同的结构元件，并解释了为什么凝血酶切割会激活该基序。

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