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1ll8

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Revision as of 07:43, 31 January 2018

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

Structural highlights

1ll8 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Transferase, with EC number 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:12377121^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wilson WA, Skurat AV, Probst B, de Paoli-Roach A, Roach PJ, Rutter J. Control of mammalian glycogen synthase by PAS kinase. Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16596-601. Epub 2005 Nov 7. PMID:16275910 doi:10.1073/pnas.0508481102
↑ An R, da Silva Xavier G, Hao HX, Semplici F, Rutter J, Rutter GA. Regulation by Per-Arnt-Sim (PAS) kinase of pancreatic duodenal homeobox-1 nuclear import in pancreatic beta-cells. Biochem Soc Trans. 2006 Nov;34(Pt 5):791-3. PMID:17052199 doi:10.1042/BST0340791
↑ Eckhardt K, Troger J, Reissmann J, Katschinski DM, Wagner KF, Stengel P, Paasch U, Hunziker P, Borter E, Barth S, Schlafli P, Spielmann P, Stiehl DP, Camenisch G, Wenger RH. Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1. Cell Physiol Biochem. 2007;20(1-4):227-40. PMID:17595531 doi:10.1159/000104169
↑ da Silva Xavier G, Farhan H, Kim H, Caxaria S, Johnson P, Hughes S, Bugliani M, Marselli L, Marchetti P, Birzele F, Sun G, Scharfmann R, Rutter J, Siniakowicz K, Weir G, Parker H, Reimann F, Gribble FM, Rutter GA. Per-arnt-sim (PAS) domain-containing protein kinase is downregulated in human islets in type 2 diabetes and regulates glucagon secretion. Diabetologia. 2011 Apr;54(4):819-27. doi: 10.1007/s00125-010-2010-7. Epub 2010, Dec 23. PMID:21181396 doi:10.1007/s00125-010-2010-7
↑ Schlafli P, Troger J, Eckhardt K, Borter E, Spielmann P, Wenger RH. Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN. FEBS J. 2011 May;278(10):1757-68. doi: 10.1111/j.1742-4658.2011.08100.x. Epub, 2011 Apr 8. PMID:21418524 doi:10.1111/j.1742-4658.2011.08100.x
↑ Kikani CK, Antonysamy SA, Bonanno JB, Romero R, Zhang FF, Russell M, Gheyi T, Iizuka M, Emtage S, Sauder JM, Turk BE, Burley SK, Rutter J. Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation. J Biol Chem. 2010 Dec 24;285(52):41034-43. Epub 2010 Oct 13. PMID:20943661 doi:10.1074/jbc.M110.157594
↑ Amezcua CA, Harper SM, Rutter J, Gardner KH. Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation. Structure. 2002 Oct;10(10):1349-61. PMID:12377121

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ll8"

@@ Line 1: / Line 1: @@
 ==Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation==
 <StructureSection load='1ll8' size='340' side='right' caption='[[1ll8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1ll8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LL8 FirstGlance]. <br>
 </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://pdbe.org/1ll8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ll8 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=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://pdbe.org/1ll8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ll8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ll8 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1ll8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1ll8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1ll8

From Proteopedia

Revision as of 07:43, 31 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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