1FHR

SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE

1FHR の概要

• エントリーDOI: 10.2210/pdb1fhr/pdb
• 関連するPDBエントリー: 1DMZ 1FHQ 1QU5
• 分子名称: PROTEIN KINASE SPK1, DNA REPAIR PROTEIN RAD9 (2 entities in total)
• 機能のキーワード: fha domain, rad53, rad9, phosphotyrosine, phosphoprotein, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Nucleus: P22216 P14737
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19158.71

構造登録者

Byeon, I.-J.L.,Liao, H.,Yongkiettrakul, S.,Tsai, M.-D. (登録日: 2000-08-02, 公開日: 2000-10-18, 最終更新日: 2024-10-30)

主引用文献

Wang, P.,Byeon, I.J.,Liao, H.,Beebe, K.D.,Yongkiettrakul, S.,Pei, D.,Tsai, M.D.
II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides.
J.Mol.Biol., 302:927-940, 2000

PubMed Abstract: The forkhead-associated (FHA) domain is a protein module found in many proteins involved in cell signaling in response to DNA damage. It has been suggested to bind to pThr sites of its target protein. Recently we have determined the first structure of an FHA domain, FHA2 from the yeast protein Rad53, and demonstrated that FHA2 binds to a pTyr-containing peptide (826)EDI(pY)YLD(832) from Rad9, with a moderate affinity (K(d) ca. 100 microM). We now report the solution structure of the complex of FHA2 bound with this pTyr peptide. The structure shows that the phosphate group of pTyr interacts directly with three arginine residues (605, 617, and 620), and that the leucine residue at the +2 position from the pTyr interacts with a hydrophobic surface on FHA2. The sequence specificity of FHA2 was determined by screening a combinatorial pTyr library. The results clearly show that FHA2 recognizes specific sequences C-terminal to pTyr with the following consensus: XX(pY)N(1)N(2)N(3), where N(1)=Leu, Met, Phe, or Ile, N(2)=Tyr, Phe, Leu, or Met, and N(3)=Phe, Leu, or Met. Two of the selected peptides, GF(pY)LYFIR and DV(pY)FYMIR, bind FHA2 with K(d) values of 1.1 and 5.0 microM, respectively. The results, along with other recent reports, demonstrate that the FHA domain is a new class of phosphoprotein-binding domain, capable of binding both pTyr and pThr sequences.

PubMed: 10993733
DOI: 10.1006/jmbi.2000.4095

実験手法

SOLUTION NMR