Jabeen, Talat and Leonard, Philip and Jamaluddin, Haryati and Acharya, K. Ravi (2008) Structure of mouse IP-10, a chemokine. Acta Crystallographica Section D Biological Crystallography, D64 . pp. 611-619. ISSN 0907-4449
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Official URL: http://dx.doi.org/10.1107/S0907444908007026
Interferon--inducible protein (IP-10) belongs to the CXC class of chemokines and plays a significant role in the pathophysiology of various immune and inflammatory responses. It is also a potent angiostatic factor with antifibrotic properties. The biological activities of IP-10 are exerted by interactions with the G-protein-coupled receptor CXCR3 expressed on Th1 lymphocytes. IP-10 thus forms an attractive target for structure-based rational drug design of antiinflammatory molecules. The crystal structure of mouse IP-10 has been determined and reveals a novel tetrameric association. In the tetramer, two conventional CXC chemokine dimers are associated through their N-terminal regions to form a 12-stranded elongated -sheet of 90 A Â° in length. This association differs significantly from the previously studied tetramers of human IP-10, platelet factor 4 and neutrophilactivating peptide-2. In addition, heparin- and receptorbinding residues were mapped on the surface of IP-10 tetramer. Two heparin-binding sites were observed on the surface and were present at the interface of each of the two -sheet dimers. The structure supports the formation of higher order oligomers of IP-10, as observed in recent in vivo studies with mouse IP-10, which will have functional relevance.
|Uncontrolled Keywords:||interferon, inducible protein, chemokines|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Deposited By:||Ms Zalinda Shuratman|
|Deposited On:||20 Nov 2008 07:04|
|Last Modified:||20 Nov 2008 07:04|
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