1LUI

NMR Structures of Itk SH2 domain, Pro287cis isoform, ensemble of 20 low energy structures

1LUI の概要

• エントリーDOI: 10.2210/pdb1lui/pdb
• 関連するPDBエントリー: 1LUK 1LUM 1LUN
• NMR情報: BMRB: 5461
• 分子名称: Tyrosine-protein kinase ITK/TSK (1 entity in total)
• 機能のキーワード: sh2 domain, cis/trans isomerization, proline, itk, tsk, t-cell, transferase
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane: Q03526
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12558.25

構造登録者

Mallis, R.J.,Brazin, K.N.,Fulton, B.F.,Andreotti, A.M. (登録日: 2002-05-22, 公開日: 2002-11-27, 最終更新日: 2024-11-20)

主引用文献

Mallis, R.J.,Brazin, K.N.,Fulton, D.B.,Andreotti, A.H.
Structural characterization of a proline-driven conformational switch within the Itk SH2 domain
Nat.Struct.Biol., 9:900-905, 2002

PubMed Abstract: Interleukin-2 tyrosine kinase (Itk) is a T cell-specific kinase required for a proper immune response following T cell receptor engagement. In addition to the kinase domain, Itk is composed of several noncatalytic regulatory domains, including a Src homology 2 (SH2) domain that contains a conformationally heterogeneous Pro residue. Cis-trans isomerization of a single prolyl imide bond within the SH2 domain mediates conformer-specific ligand recognition that may have functional implications in T cell signaling. To better understand the mechanism by which a proline switch regulates ligand binding, we have used NMR spectroscopy to determine two structures of Itk SH2 corresponding to the cis and trans imide bond-containing conformers. The structures indicate that the heterogeneous Pro residue acts as a hinge that modulates ligand recognition by controlling the relative orientation of protein-binding surfaces.

PubMed: 12402030
DOI: 10.1038/nsb864

実験手法

SOLUTION NMR