2L9H

Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data

2L9H の概要

• エントリーDOI: 10.2210/pdb2l9h/pdb
• 関連するPDBエントリー: 1u4l
• NMR情報: BMRB: 17453
• 分子名称: C-C motif chemokine 5 (1 entity in total)
• 機能のキーワード: immune system, chemokine, oligomer
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P13501
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 31448.04

構造登録者

Wang, X.,Watson, C.M.,Sharp, J.S.,Handel, T.M.,Prestegard, J.H. (登録日: 2011-02-09, 公開日: 2011-06-22, 最終更新日: 2024-11-27)

主引用文献

Wang, X.,Watson, C.,Sharp, J.S.,Handel, T.M.,Prestegard, J.H.
Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data.
Structure, 19:1138-1148, 2011

PubMed Abstract: CCL5 (RANTES) is a proinflammatory chemokine known to activate leukocytes through its receptor, CCR5. Although the monomeric form of CCL5 is sufficient to cause cell migration in vitro, CCL5's propensity for aggregation is essential for migration in vivo, T cell activation and apoptosis, and HIV entry into cells. However, there is currently no structural information on CCL5 oligomers larger than the canonical CC chemokine dimer. In this study the solution structure of a CCL5 oligomer was investigated using an integrated approach, including NMR residual dipolar couplings to determine allowed relative orientations of the component monomers, SAXS to restrict overall shape, and hydroxyl radical footprinting and NMR cross-saturation experiments to identify interface residues. The resulting model of the CCL5 oligomer provides a basis for explaining the disaggregating effect of E66 and E26 mutations and suggests mechanisms by which glycosaminoglycan binding may promote oligomer formation and facilitate cell migration in vivo.

PubMed: 21827949
DOI: 10.1016/j.str.2011.06.001

実験手法

SOLUTION NMR
SOLUTION SCATTERING