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Crystal structure of IP-10 T-formCrystal structure of IP-10 T-form
Structural highlights
Function[CXL10_HUMAN] Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the structure of wild-type IP-10 from three crystal forms. The crystals provide eight separate models of the IP-10 chain, all differing substantially from a monomeric IP-10 variant examined previously by NMR spectroscopy. In each crystal form, IP-10 chains form conventional beta sheet dimers, which, in turn, form a distinct tetrameric assembly. The M form tetramer is reminiscent of platelet factor 4, whereas the T and H forms feature a novel twelve-stranded beta sheet. Analytical ultracentrifugation indicates that, in free solution, IP-10 exists in a monomer-dimer equilibrium with a dissociation constant of 9 microM. We propose that the tetrameric structures may represent species promoted by the binding of glycosaminoglycans. The binding sites for several IP-10-neutralizing mAbs have also been mapped. Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine.,Swaminathan GJ, Holloway DE, Colvin RA, Campanella GK, Papageorgiou AC, Luster AD, Acharya KR Structure. 2003 May;11(5):521-32. PMID:12737818[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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