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*

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

2 Citations (Scopus)


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
Issue number3
Publication statusPublished - Mar 2018

Scopus Subject Areas

  • Physics and Astronomy(all)

User-Defined Keywords

  • CXCR1-IL8 complex
  • homology modeling
  • ligand binding
  • molecular dynamics


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