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| [[Image:1u4m.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1u4m| PDB=1u4m | SCENE= }} | | {{STRUCTURE_1u4m| PDB=1u4m | SCENE= }} |
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| '''human RANTES complexed to heparin-derived disaccharide III-S'''
| | ===human RANTES complexed to heparin-derived disaccharide III-S=== |
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| ==Overview==
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| The biological activity of chemokines requires interactions with cell surface proteoglycans. We have determined the structure of the chemokine RANTES (regulated on activation normal T cell expressed) in the presence of heparin-derived disaccharide analogs by X-ray crystallography. These structures confirm the essential role of the BBXB motif in the interaction between the chemokine and the disaccharide. Unexpected interactions were observed in the 30s loop and at the amino terminus. Mutant RANTES molecules were designed to abrogate these interactions and their biological activity examined in vivo. The K45E mutant within the BBXB motif lost the capacity to bind heparin and the ability to elicit cellular recruitment. The Y3A mutant maintained its capacity to bind heparin but was unable to elicit cellular recruitment. Finally, a tetrasaccharide is the smallest oligosaccharide which effectively abolishes the ability of RANTES to recruit cells in vivo. These crystallographic structures provide a description of the molecular interaction of a chemokine with glycosaminoglycans. | | The line below this paragraph, {{ABSTRACT_PUBMED_15530372}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15530372 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15530372}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Protein-heparin disaccharide complex]] | | [[Category: Protein-heparin disaccharide complex]] |
| [[Category: Rante]] | | [[Category: Rante]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:45:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:50:22 2008'' |
