1o7z: Difference between revisions

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==Overview==
==Overview==
We 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.
We 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.


==About this Structure==
==About this Structure==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12737818 12737818]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12737818 12737818]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Acharya, K.R.]]
[[Category: Acharya, K R.]]
[[Category: Holloway, D.E.]]
[[Category: Holloway, D E.]]
[[Category: Papageorgiou, A.C.]]
[[Category: Papageorgiou, A C.]]
[[Category: Swaminathan, G.J.]]
[[Category: Swaminathan, G J.]]
[[Category: chemokine]]
[[Category: chemokine]]
[[Category: chemotaxis]]
[[Category: chemotaxis]]
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[[Category: interferon induction]]
[[Category: interferon induction]]


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Revision as of 15:14, 21 February 2008

File:1o7z.jpg


1o7z, resolution 1.92Å

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CRYSTAL STRUCTURE OF IP-10 T-FORM

OverviewOverview

We 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.

About this StructureAbout this Structure

1O7Z is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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

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