2R3Z

Crystal structure of mouse IP-10

Summary for 2R3Z

• Entry DOI: 10.2210/pdb2r3z/pdb
• Related: 1O7Y 1O7Z 1O80
• Descriptor: Small-inducible cytokine B10 (2 entities in total)
• Functional Keywords: ip-10/cxcl10, chemokine, chemotaxis, inflammatory response, attractant
• Biological source: Mus musculus (Mouse)
• Cellular location: Secreted: P17515
• Total number of polymer chains: 4
• Total formula weight: 30700.82

Authors

Jabeen, T.,Leonard, P.,Jamaluddin, H.,Acharya, K.R. (deposition date: 2007-08-30, release date: 2008-08-12, Last modification date: 2024-10-30)

Primary citation

Jabeen, T.,Leonard, P.,Jamaluddin, H.,Acharya, K.R.
Structure of mouse IP-10, a chemokine
Acta Crystallogr.,Sect.D, 64:611-619, 2008

PubMed 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 approximately 90 A 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.

PubMed: 18560148
DOI: 10.1107/S0907444908007026

Experimental method

X-RAY DIFFRACTION (2.5 Å)