2b9f: Difference between revisions

Revision as of 17:35, 21 February 2008

Crystal structure of non-phosphorylated Fus3

OverviewOverview

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.

About this StructureAbout this Structure

2B9F is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network., Remenyi A, Good MC, Bhattacharyya RP, Lim WA, Mol Cell. 2005 Dec 22;20(6):951-62. PMID:16364919

Page seeded by OCA on Thu Feb 21 16:35:33 2008

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OCA

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-[[Image:2b9f.gif|left|200px]]<br /><applet load="2b9f" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2b9f.gif|left|200px]]<br /><applet load="2b9f" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2b9f, resolution 1.8&Aring;" />
 '''Crystal structure of non-phosphorylated Fus3'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-B9F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B9F OCA].
+B9F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B9F OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Bhattacharyya, R.P.]]
+[[Category: Bhattacharyya, R P.]]
-[[Category: Good, M.C.]]
+[[Category: Good, M C.]]
-[[Category: Lim, W.A.]]
+[[Category: Lim, W A.]]
 [[Category: Remenyi, A.]]
 [[Category: ADP]]
@@ Line 22: / Line 22: @@
 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:39:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:33 2008''