Structural highlights
Function
[CXL10_HUMAN] Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of IP-10 was solved by NMR spectroscopy and represents the first structure from the class of agonists toward the receptor CXCR3. CXCR3 binding chemokines are unique in their ability to bind receptors from both the CC and CXC classes of chemokine receptors. An unusual structural feature of IP-10 was identified that may provide the basis for the ability of IP-10 to bind both CXCR3 and CCR3. The surface of IP-10 that interacts with the N-terminus of CXCR3 was defined by monitoring changes in the NMR spectrum of IP-10 upon addition of a CXCR3 N-terminal peptide. These studies indicated that the interaction involves a hydrophobic cleft, formed by the N-loop and 40s-loop region of IP-10, similar to the interaction surface observed for other chemokines such as IL-8. An additional region of interaction was observed that consists of a hydrophobic cleft formed by the N-terminus of IP-10 and 30s-loop of IP-10.
The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions.,Booth V, Keizer DW, Kamphuis MB, Clark-Lewis I, Sykes BD Biochemistry. 2002 Aug 20;41(33):10418-25. PMID:12173928[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Booth V, Keizer DW, Kamphuis MB, Clark-Lewis I, Sykes BD. The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions. Biochemistry. 2002 Aug 20;41(33):10418-25. PMID:12173928
