5WDZ

Structure of monomeric Interleukin-8 (1-66)

5WDZ の概要

• エントリーDOI: 10.2210/pdb5wdz/pdb
• NMR情報: BMRB: 30316
• 分子名称: Interleukin-8 (1 entity in total)
• 機能のキーワード: interleukin-8, chemokine-fold, cytokine
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7714.06

構造登録者

Berkamp, S.,Opella, S.J.,Marassi, F.M. (登録日: 2017-07-06, 公開日: 2017-11-29, 最終更新日: 2024-10-16)

主引用文献

Berkamp, S.,Park, S.H.,De Angelis, A.A.,Marassi, F.M.,Opella, S.J.
Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.
J. Biomol. NMR, 69:111-121, 2017

PubMed 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.

PubMed: 29143165
DOI: 10.1007/s10858-017-0128-3

実験手法

SOLUTION NMR