1QE6

INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)

1QE6 の概要

• エントリーDOI: 10.2210/pdb1qe6/pdb
• 関連するPDBエントリー: 1ICW 3IL8
• 分子名称: INTERLEUKIN-8 VARIANT, SULFATE ION (3 entities in total)
• 機能のキーワード: intercrine alpha family, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P10145
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 33715.34

構造登録者

Gerber, N.,Lowman, H.,Artis, D.R.,Eigenbrot, C. (登録日: 1999-07-13, 公開日: 2000-03-22, 最終更新日: 2018-01-31)

主引用文献

Gerber, N.,Lowman, H.,Artis, D.R.,Eigenbrot, C.
Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution.
Proteins, 38:361-367, 2000

PubMed Abstract: The "ELR" (Glu-Leu-Arg) tripeptide sequence near the N-terminus of interleukin-8 (IL-8) contributes a large part of the receptor binding free energy. Prior X-ray and nuclear magnetic resonance (NMR) structures of IL-8 have shown this region of the molecule to be highly mobile. We reasoned that a hydrophobic interaction between the leucine and the neighboring beta-turn might exist in the receptor binding conformation of the N-terminus. To test this hypothesis, we mutated two residues to cysteine and connected the N-terminus to the beta-turn. The mutant retains receptor binding affinity reasonably close to wild type and allows the characterization of a high-affinity conformation that may be useful in the design of small IL-8 mimics. The L5C/H33C mutant is refined to R-values of R = 20.6% and Rfree = 27.7% at 2.35 A resolution. Other receptor binding determinants reside in the "N-loop" found after "ELR" and preceding the first beta-strand. All available structures of IL-8 have been found with one of two distinct N-loop conformations. One of these is relevant for receptor binding, based on NMR results with receptor peptides. The other conformation obscures the receptor-peptide binding surface and may have an undetermined but necessarily different function.

PubMed: 10707023
DOI: 10.1002/(SICI)1097-0134(20000301)38:4<361::AID-PROT2>3.3.CO;2-S

実験手法

X-RAY DIFFRACTION (2.35 Å)