Research

Structure of mouse IP-10, a chemokine


Reference:

Jabeen, T., Leonard, P., Jamaluddin, H. and Acharya, K. R., 2008. Structure of mouse IP-10, a chemokine. Acta Crystallographica Section D-Biological Crystallography, 64, pp. 611-619.

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Official URL:

http://dx.doi.org/10.1107/S0907444908007026

Abstract

Interferon-gamma-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 anti-inflammatory 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 beta-sheet of similar to 90 angstrom in length. This association differs significantly from the previously studied tetramers of human IP-10, platelet factor 4 and neutrophil-activating peptide-2. In addition, heparin- and receptor-binding 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 beta-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.

Details

Item Type Articles
CreatorsJabeen, T., Leonard, P., Jamaluddin, H. and Acharya, K. R.
DOI10.1107/s0907444908007026
DepartmentsFaculty of Engineering & Design > Electronic & Electrical Engineering
Faculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code5663

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