Molecular approaches to structure-function analysis of interleukin-8
Methods in Enzymology, ISSN: 0076-6879, Vol: 287, Page: 45-58
1997
- 10Citations
- 3Captures
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Metrics Details
- Citations10
- Citation Indexes10
- CrossRef10
- Captures3
- Readers3
Article Description
By constructing and measuring receptor-binding affinities of IL-8 and melanoma growth stimulating activity variants, this chapter shows that the N-loop region of IL-8 is required for binding to CXCR1. The conformation of the N-loop appears critical for CXCR1 binding, based on the need for Leu-49, which packs against the N-loop residues Tyr-13 and Phe-17. The N-terminal domains of CXCR1 and CXCR2 have been previously shown to interact with IL-8 and to play a role in determining chemokine-binding specificity. The N-loop region of IL-8 therefore, interacts directly with the N-terminal domains of the IL-8 receptors. Based on the available data the chapter speculates that there is a one-to-one interaction of the secondary N-loop site on IL-8 with a portion of the CXCR1 N-terminal domain and that the ELR residues interact with a region of charged residues, Arg-199, Arg-203, and Asp-265, identified by alanine scanning mutagenesis in CXCRI extracellular loops 3 and 4.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0076687997870061; http://dx.doi.org/10.1016/s0076-6879(97)87006-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0030632969&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9330314; https://linkinghub.elsevier.com/retrieve/pii/S0076687997870061; http://linkinghub.elsevier.com/retrieve/pii/S0076687997870061; http://dx.doi.org/10.1016/s0076-6879%2897%2987006-1; https://dx.doi.org/10.1016/s0076-6879%2897%2987006-1
Elsevier BV
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