CXCR3 Structure

CXCR3 Structure

The ability of CXCR3 (CXCR3 antibody) binding chemokines to bind receptors from both the CC and CXC classes of chemokine receptors makes them unique. IP-10 has an interesting structural property that may explain its ability to bind to CXCR3 and CCR3. By monitoring changes in the NMR spectra of IP-10 after adding a CXCR3 N-terminal peptide, the surface of IP-10 that interacts with the N-terminus of CXCR3 was determined. According to this research, the interaction involves a hydrophobic gap produced by IP-10's N-loop and 40s-loop regions, which is similar to the interaction surface seen for other chemokines like IL-8. A hydrophobic gap created between the N-terminus of IP-10 and the 30s-loop of IP-10 was discovered as an additional site of contact.

The gene encoding the murine homolog of human CXCR3 occurs in a single copy with two exons and an intron between nucleotides 10 and 11 disrupting the coding region. The anticipated human sequence is 86 percent identical to the derived amino acid sequence. CXCR3 mRNA is detected in bone marrow cells cultivated in the presence of IL-2, but not in cells that have not been activated. It's also found in small amounts in the spleen, lymph nodes, mammary gland, and thymus of normal mice.