Structure of mouse IP-10, a chemokine


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.

Related documents:

This repository does not currently have the full-text of this item.
You may be able to access a copy if URLs are provided below. (Contact Author)

Official URL:

Related URLs:


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.


Item Type Articles
CreatorsJabeen, T., Leonard, P., Jamaluddin, H. and Acharya, K. R.
Related URLs
DepartmentsFaculty of Engineering & Design > Electronic & Electrical Engineering
Faculty of Science > Biology & Biochemistry
ID Code5663


Actions (login required)

View Item