2B9H

Crystal structure of Fus3 with a docking motif from Ste7

2B9H の概要

• エントリーDOI: 10.2210/pdb2b9h/pdb
• 関連するPDBエントリー: 2B9F 2B9I 2B9J
• 分子名称: Mitogen-activated protein kinase FUS3, Serine/threonine-protein kinase STE7, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Nucleus: P16892
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42924.48

構造登録者

Remenyi, A.,Good, M.C.,Bhattacharyya, R.P.,Lim, W.A. (登録日: 2005-10-11, 公開日: 2006-01-03, 最終更新日: 2023-08-23)

主引用文献

Remenyi, A.,Good, M.C.,Bhattacharyya, R.P.,Lim, W.A.
The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network.
Mol.Cell, 20:951-962, 2005

PubMed Abstract: Cells use a network of mitogen-activated protein kinases (MAPKs) to coordinate responses to diverse extracellular signals. Here, we examine the role of docking interactions in determining connectivity of the yeast MAPKs Fus3 and Kss1. These closely related kinases are activated by the common upstream MAPK kinase Ste7 yet generate distinct output responses, mating and filamentous growth, respectively. We find that docking interactions are necessary for communication with the kinases and that they can encode subtle differences in pathway-specific input and output. The cell cycle arrest mediator Far1, a mating-specific substrate, has a docking motif that selectively binds Fus3. In contrast, the shared partner Ste7 has a promiscuous motif that binds both Fus3 and Kss1. Structural analysis reveals that Fus3 interacts with specific and promiscuous peptides in conformationally distinct modes. Induced fit recognition may allow docking peptides to achieve discrimination by exploiting subtle differences in kinase flexibility.

PubMed: 16364919
DOI: 10.1016/j.molcel.2005.10.030

実験手法

X-RAY DIFFRACTION (1.55 Å)