Structural diversity of heparan sulfate binding domains in chemokines

被引:204
作者
Lortat-Jacob, H
Grosdidier, A
Imberty, A
机构
[1] Univ Grenoble 1, CNRS, CEA, Inst Biol Struct,Lab Biophys Mol, F-38027 Grenoble 01, France
[2] Univ Grenoble 1, CNRS, Ctr Rech Macromol Vegetales, F-38041 Grenoble 09, France
关键词
D O I
10.1073/pnas.032497699
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Heparan sulfate (HS) molecules are ubiquitous in animal tissues where they function as ligands that are dramatically involved in the regulation of the proteins they bind. Of these, chemokines are a family of small proteins with many biological functions. Their well-conserved monomeric structure can associate in various oligomeric forms especially in the presence of HS. Application of protein surface analysis and energy calculations to all known chemokine structures leads to the proposal that four different binding modes are created by the folding and oligomerization of these proteins. So, based on the present state of our knowledge, four different clusters of amino acids should be involved in the recognition process. Our results help to rationalize how unique sequences of HS specifically bind any given chemokine. The conclusions open the route for a rational design of compounds of therapeutical interest that could influence chemokine activity.
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收藏
页码:1229 / 1234
页数:6
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