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J Biomol NMR. 2017 Nov;69(3):111-121. doi: 10.1007/s10858-017-0128-3. Epub 2017 Nov 15.

Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.

Author information

1
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA.
2
Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, San Diego, CA, 92037, USA.
3
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA. sopella@ucsd.edu.

Abstract

The structure of monomeric human chemokine IL-8 (residues 1-66) was determined in aqueous solution by NMR spectroscopy. The structure of the monomer is similar to that of each subunit in the dimeric full-length protein (residues 1-72), with the main differences being the location of the N-loop (residues 10-22) relative to the C-terminal α-helix and the position of the side chain of phenylalanine 65 near the truncated dimerization interface (residues 67-72). NMR was used to analyze the interactions of monomeric IL-8 (1-66) with ND-CXCR1 (residues 1-38), a soluble polypeptide corresponding to the N-terminal portion of the ligand binding site (Binding Site-I) of the chemokine receptor CXCR1 in aqueous solution, and with 1TM-CXCR1 (residues 1-72), a membrane-associated polypeptide that includes the same N-terminal portion of the binding site, the first trans-membrane helix, and the first intracellular loop of the receptor in nanodiscs. The presence of neither the first transmembrane helix of the receptor nor the lipid bilayer significantly affected the interactions of IL-8 with Binding Site-I of CXCR1.

KEYWORDS:

CXCL8; Chemokine; GPCR; IL-8; Nanodisc; Protein structure

PMID:
29143165
PMCID:
PMC5869024
DOI:
10.1007/s10858-017-0128-3
[Indexed for MEDLINE]
Free PMC Article

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