Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1YRK

The C2 Domain of PKC is a new Phospho-Tyrosine Binding Domain

1YRK の概要
エントリーDOI10.2210/pdb1yrk/pdb
関連するPDBエントリー1BDY
分子名称Protein kinase C, delta type, 13-residue peptide, ACETIC ACID, ... (4 entities in total)
機能のキーワードc2 domain, protein binding
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cytoplasm (By similarity): Q05655
タンパク質・核酸の鎖数2
化学式量合計15993.29
構造登録者
Benes, C.H.,Wu, N.,Elia, A.E.,Dharia, T.,Cantley, L.C.,Soltoff, S.P. (登録日: 2005-02-03, 公開日: 2005-07-26, 最終更新日: 2011-07-13)
主引用文献Benes, C.H.,Wu, N.,Elia, A.E.,Dharia, T.,Cantley, L.C.,Soltoff, S.P.
The C2 domain of PKCdelta is a phosphotyrosine binding domain.
Cell(Cambridge,Mass.), 121:271-280, 2005
Cited by
PubMed Abstract: In this issue of Cell, report that the C2 domain of the serine/threonine protein kinase Cdelta is a phosphotyrosine binding domain and present the crystal structure of this C2 domain bound to a peptide containing phosphotyrosine. Prior to this work, C2 domains were thought to bind only to phospholipids or to unphosphorylated proteins, and the SH2 and PTB domains were the only signaling domains known to recognize phosphotyrosine. This new role for the C2 domain links phosphotyrosine recognition directly to serine/threonine kinase activity and reveals an unexpected mechanism for crosstalk between distinct signaling pathways.
PubMed: 15851022
DOI: 10.1016/j.cell.2005.02.019
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 1yrk
検証レポート(詳細版)ダウンロードをダウンロード

227111

件を2024-11-06に公開中

PDB statisticsPDBj update infoContact PDBjnumon