1ll8

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[[Image:1ll8.gif|left|200px]]
 
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{{Structure
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==Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation==
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|PDB= 1ll8 |SIZE=350|CAPTION= <scene name='initialview01'>1ll8</scene>
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<StructureSection load='1ll8' size='340' side='right'caption='[[1ll8]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ll8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LL8 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [https://pdbe.org/1ll8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ll8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ll8 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://www.ebi.ac.uk/pdbsum/1ll8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB]</span>
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[https://www.uniprot.org/uniprot/PASK_HUMAN PASK_HUMAN] Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation.<ref>PMID:16275910</ref> <ref>PMID:17052199</ref> <ref>PMID:17595531</ref> <ref>PMID:21181396</ref> <ref>PMID:21418524</ref> <ref>PMID:20943661</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1ll8_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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PAS domains are sensory modules in signal-transducing proteins that control responses to various environmental stimuli. To examine how those domains can regulate a eukaryotic kinase, we have studied the structure and binding interactions of the N-terminal PAS domain of human PAS kinase using solution NMR methods. While this domain adopts a characteristic PAS fold, two regions are unusually flexible in solution. One of these serves as a portal that allows small organic compounds to enter into the core of the domain, while the other binds and inhibits the kinase domain within the same protein. Structural and functional analyses of point mutants demonstrate that the compound and ligand binding regions are linked, suggesting that the PAS domain serves as a ligand-regulated switch for this eukaryotic signaling system.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</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=1ll8 ConSurf].
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1LL8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL8 OCA].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation., Amezcua CA, Harper SM, Rutter J, Gardner KH, Structure. 2002 Oct;10(10):1349-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12377121 12377121]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Amezcua CA]]
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[[Category: Amezcua, C A.]]
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[[Category: Gardner KH]]
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[[Category: Gardner, K H.]]
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[[Category: Harper SM]]
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[[Category: Harper, S M.]]
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[[Category: Rutter J]]
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[[Category: Rutter, J.]]
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[[Category: kinase regulation]]
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[[Category: ligand binding]]
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[[Category: ligand screening]]
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[[Category: pas domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:10 2008''
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Current revision

Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation

PDB ID 1ll8

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