A computational study of the chemokine receptor CXCR1 bound with interleukin-8

Yang Wang, Cecylia Severin Lupala, Ting Wang, Xuanxuan Li, Ji Hye Yun, Jae Hyun Park, Zeyu Jin, Weontae Lee, Leihan Tan, Haiguang Liu

Research output: Contribution to journalArticle

Abstract

CXCR1 is a G-protein coupled receptor, transducing signals from chemokines, in particular the interleukin-8 (IL8) molecules. This study combines homology modeling and molecular dynamics simulation methods to study the structure of CXCR1-IL8 complex. By using CXCR4-vMIP-II crystallography structure as the homologous template, CXCR1-IL8 complex structure was constructed, and then refined using all-atom molecular dynamics simulations. Through extensive simulations, CXCR1-IL8 binding poses were investigated in detail. Furthermore, the role of the N-terminal of CXCR1 receptor was studied by comparing four complex models differing in the N-terminal sequences. The results indicate that the receptor N-terminal affects the binding of IL8 significantly. With a shorter N-terminal domain, the binding of IL8 to CXCR1 becomes unstable. The homology modeling and simulations also reveal the key receptor-ligand residues involved in the electrostatic interactions known to be vital for complex formation.

Original languageEnglish
Article number038702
JournalChinese Physics B
Volume27
Issue number3
DOIs
Publication statusPublished - 2018 Mar

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)

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    Wang, Y., Severin Lupala, C., Wang, T., Li, X., Yun, J. H., Park, J. H., Jin, Z., Lee, W., Tan, L., & Liu, H. (2018). A computational study of the chemokine receptor CXCR1 bound with interleukin-8. Chinese Physics B, 27(3), [038702]. https://doi.org/10.1088/1674-1056/27/3/038702