1VMC

STROMA CELL-DERIVED FACTOR-1ALPHA (SDF-1ALPHA)

1VMC の概要

• エントリーDOI: 10.2210/pdb1vmc/pdb
• 分子名称: Stromal cell-derived factor 1 (1 entity in total)
• 機能のキーワード: cxc-chemokine, cytokine
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P48061
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8343.80

構造登録者

Gozansky, E.K.,Clore, G.M. (登録日: 2004-09-20, 公開日: 2005-03-01, 最終更新日: 2024-11-13)

主引用文献

Gozansky, E.K.,Louis, J.M.,Caffrey, M.,Clore, G.M.
Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha.
J.Mol.Biol., 345:651-658, 2005

PubMed Abstract: The solution structure of monomeric stromal cell-derived factor-1alpha (SDF-1alpha), the natural ligand for the CXCR4 G-coupled receptor, has been solved by multidimensional heteronuclear NMR spectroscopy. The structure has a characteristic chemokine fold and is in excellent agreement with the individual subunits observed in the crystal structures of dimeric SDF-1alpha. Using various peptides derived from the N-terminal extracellular tail of the CXCR4 receptor, we show that the principal determinants of binding reside in the N-terminal 17 residues of CXCR4, with a major contribution from the first six residues. From 15N/1HN chemical shift pertubation studies we show that the interaction surface on SDF-1alpha is formed by the undersurface of the three-stranded antiparallel beta-sheet bounded by the N-terminal loop on one side and the C-terminal helix on the other. This surface overlaps with but is not identical to that mapped on several other chemokines for the binding of equivalent peptides derived from their respective receptors.

PubMed: 15588815
DOI: 10.1016/j.jmb.2004.11.003

実験手法

SOLUTION NMR