The CXCR3 Binding Chemokine IP-10/CXCL10: Structure and Receptor Interactions
| Autor: | Ian Clark-Lewis, Valerie Booth, David W. Keizer, B.D. Sykes, Monique B Kamphuis |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Chemokine Receptors CXCR3 Stereochemistry CCR3 Plasma protein binding CXCR3 Biochemistry Protein Structure Secondary Chemokine receptor Protein structure immune system diseases Humans Receptor Nuclear Magnetic Resonance Biomolecular CXCL16 Nitrogen Isotopes biology hemic and immune systems Peptide Fragments Chemokine CXCL10 biology.protein Receptors Chemokine Protons Chemokines CXC Dimerization Protein Binding |
| Zdroj: | Biochemistry. 41:10418-10425 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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