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PDBsum entry 2b9h

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
2b9h
Contents
Protein chains
337 a.a.
12 a.a.
Ligands
ADP
Metals
_MG
Waters ×391

References listed in PDB file
Key reference
Title The role of docking interactions in mediating signaling input, Output, And discrimination in the yeast mapk network.
Authors A.Reményi, M.C.Good, R.P.Bhattacharyya, W.A.Lim.
Ref. Mol Cell, 2005, 20, 951-962. [DOI no: 10.1016/j.molcel.2005.10.030]
PubMed id 16364919
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.
Figure 1.
Figure 1. Docking Motifs Found in Interaction Partners of the Saccharomyces cerevisiae MAPKs Fus3 and Kss1
Figure 3.
Figure 3. Structure of the Fus3 MAPK
The above figures are reprinted by permission from Cell Press: Mol Cell (2005, 20, 951-962) copyright 2005.
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