1QJA

14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)

1QJA の概要

• エントリーDOI: 10.2210/pdb1qja/pdb
• 関連するPDBエントリー: 14PS 1A37 1A38 1A4O 1QJB
• 分子名称: 14-3-3 PROTEIN ZETA, PHOSPHOPEPTIDE (3 entities in total)
• 機能のキーワード: kinase inhibitor/peptide, complex (signal transduction-peptide), complex, 14-3-3, phosphopeptide, signal transduction, kinase inhibitor-peptide complex
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57630.37

構造登録者

Rittinger, K.,Budman, J.,Xu, J.,Volinia, S.,Cantley, L.C.,Smerdon, S.J.,Gamblin, S.J.,Yaffe, M.B. (登録日: 1999-06-23, 公開日: 1999-09-15, 最終更新日: 2024-10-16)

主引用文献

Rittinger, K.,Budman, J.,Xu, J.,Volinia, S.,Cantley, L.C.,Smerdon, S.J.,Gamblin, S.J.,Yaffe, M.B.
Structural Analysis of 14-3-3 Phosphopeptide Complexes Identifies a Dual Role for the Nuclear Export Signal of 14-3-3 in Ligand Binding
Mol.Cell, 4:153-, 1999

PubMed Abstract: We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery.

PubMed: 10488331
DOI: 10.1016/S1097-2765(00)80363-9

実験手法

X-RAY DIFFRACTION (2 Å)