2vkn
From Proteopedia
(Difference between revisions)
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<StructureSection load='2vkn' size='340' side='right' caption='[[2vkn]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='2vkn' size='340' side='right' caption='[[2vkn]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2vkn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2vkn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2qk6 2qk6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VKN FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase_kinase Mitogen-activated protein kinase kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.12.2 2.7.12.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase_kinase Mitogen-activated protein kinase kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.12.2 2.7.12.2] </span></td></tr> | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vkn RCSB], [http://www.ebi.ac.uk/pdbsum/2vkn PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vkn OCA], [http://pdbe.org/2vkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vkn RCSB], [http://www.ebi.ac.uk/pdbsum/2vkn PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/SHO1_YEAST SHO1_YEAST]] Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway.<ref>PMID:10762242</ref> <ref>PMID:10931333</ref> <ref>PMID:10970855</ref> <ref>PMID:10980703</ref> <ref>PMID:11084293</ref> <ref>PMID:11922108</ref> <ref>PMID:12455951</ref> <ref>PMID:12511654</ref> <ref>PMID:14595107</ref> <ref>PMID:15020407</ref> <ref>PMID:15200958</ref> <ref>PMID:15200959</ref> <ref>PMID:15256499</ref> <ref>PMID:16778768</ref> <ref>PMID:18480263</ref> <ref>PMID:19318625</ref> <ref>PMID:19439450</ref> <ref>PMID:7624781</ref> <ref>PMID:9180081</ref> <ref>PMID:9744864</ref> [[http://www.uniprot.org/uniprot/PBS2_YEAST PBS2_YEAST]] Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.<ref>PMID:7681220</ref> <ref>PMID:10970855</ref> <ref>PMID:15256499</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
- | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vkn ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Atcc 18824]] | ||
[[Category: Mitogen-activated protein kinase kinase]] | [[Category: Mitogen-activated protein kinase kinase]] | ||
- | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Kursula, I]] | [[Category: Kursula, I]] | ||
[[Category: Kursula, P]] | [[Category: Kursula, P]] |
Revision as of 20:16, 8 February 2016
YEAST SHO1 SH3 DOMAIN COMPLEXED WITH A PEPTIDE FROM PBS2
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