3mtl: Difference between revisions

Latest revision as of 11:06, 2 August 2023

Crystal structure of the PCTAIRE1 kinase in complex with Indirubin E804

Structural highlights

3mtl is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	FEF
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDK16_HUMAN Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro).^[1] ^[2] ^[3]

Evolutionary Conservation

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

References

↑ Shehata SN, Hunter RW, Ohta E, Peggie MW, Lou HJ, Sicheri F, Zeqiraj E, Turk BE, Sakamoto K. Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase. Cell Signal. 2012 Nov;24(11):2085-94. doi: 10.1016/j.cellsig.2012.06.018. Epub, 2012 Jul 11. PMID:22796189 doi:10.1016/j.cellsig.2012.06.018
↑ Chen XY, Gu XT, Saiyin H, Wan B, Zhang YJ, Li J, Wang YL, Gao R, Wang YF, Dong WP, Najjar SM, Zhang CY, Ding HF, Liu JO, Yu L. Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells. J Biol Chem. 2012 Aug 31;287(36):30368-75. doi: 10.1074/jbc.M112.375618. Epub, 2012 Jul 13. PMID:22798068 doi:10.1074/jbc.M112.375618
↑ Mikolcevic P, Sigl R, Rauch V, Hess MW, Pfaller K, Barisic M, Pelliniemi LJ, Boesl M, Geley S. Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis. Mol Cell Biol. 2012 Feb;32(4):868-79. doi: 10.1128/MCB.06261-11. Epub 2011 Dec, 19. PMID:22184064 doi:10.1128/MCB.06261-11

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OCA

[1] Shehata SN, Hunter RW, Ohta E, Peggie MW, Lou HJ, Sicheri F, Zeqiraj E, Turk BE, Sakamoto K. Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase. Cell Signal. 2012 Nov;24(11):2085-94. doi: 10.1016/j.cellsig.2012.06.018. Epub, 2012 Jul 11. PMID:22796189 doi:10.1016/j.cellsig.2012.06.018

[2] Chen XY, Gu XT, Saiyin H, Wan B, Zhang YJ, Li J, Wang YL, Gao R, Wang YF, Dong WP, Najjar SM, Zhang CY, Ding HF, Liu JO, Yu L. Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells. J Biol Chem. 2012 Aug 31;287(36):30368-75. doi: 10.1074/jbc.M112.375618. Epub, 2012 Jul 13. PMID:22798068 doi:10.1074/jbc.M112.375618

[3] Mikolcevic P, Sigl R, Rauch V, Hess MW, Pfaller K, Barisic M, Pelliniemi LJ, Boesl M, Geley S. Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis. Mol Cell Biol. 2012 Feb;32(4):868-79. doi: 10.1128/MCB.06261-11. Epub 2011 Dec, 19. PMID:22184064 doi:10.1128/MCB.06261-11

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='3mtl' size='340' side='right'caption='[[3mtl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mtl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3MTL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mtl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEF:(2Z,3E)-2,3-BIINDOLE-2,3(1H,1H)-DIONE+3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME}'>FEF</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEF:(2Z,3E)-2,3-BIINDOLE-2,3(1H,1H)-DIONE+3-{O-[(3R)-3,4-DIHYDROXYBUTYL]OXIME}'>FEF</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3mtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtl OCA], [http://pdbe.org/3mtl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mtl RCSB], [http://www.ebi.ac.uk/pdbsum/3mtl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtl ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtl OCA], [https://pdbe.org/3mtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mtl RCSB], [https://www.ebi.ac.uk/pdbsum/3mtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CDK16_HUMAN CDK16_HUMAN]] Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro).<ref>PMID:22796189</ref> <ref>PMID:22798068</ref> <ref>PMID:22184064</ref>
+[https://www.uniprot.org/uniprot/CDK16_HUMAN CDK16_HUMAN] Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro).<ref>PMID:22796189</ref> <ref>PMID:22798068</ref> <ref>PMID:22184064</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Cyclin-dependent kinase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Amos, A]]
+[[Category: Amos A]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Ayinampudi, V]]
+[[Category: Ayinampudi V]]
-[[Category: Berridge, G]]
+[[Category: Berridge G]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Bullock, A]]
+[[Category: Bullock A]]
-[[Category: Burgess-Brown, N]]
+[[Category: Burgess-Brown N]]
-[[Category: Das, S]]
+[[Category: Das S]]
-[[Category: Delft, F von]]
+[[Category: Edwards A]]
-[[Category: Edwards, A]]
+[[Category: Fedorov O]]
-[[Category: Fedorov, O]]
+[[Category: Filippakopoulos P]]
-[[Category: Filippakopoulos, P]]
+[[Category: Keates T]]
-[[Category: Keates, T]]
+[[Category: Knapp S]]
-[[Category: Knapp, S]]
+[[Category: Krojer T]]
-[[Category: Krojer, T]]
+[[Category: Muniz J]]
-[[Category: Muniz, J]]
+[[Category: Phillips C]]
-[[Category: Phillips, C]]
+[[Category: Pike ACW]]
-[[Category: Pike, A C.W]]
+[[Category: Rellos P]]
-[[Category: Rellos, P]]
+[[Category: Roos A]]
-[[Category: Roos, A]]
+[[Category: Savitsky P]]
-[[Category: Structural genomic]]
+[[Category: Sharpe TD]]
-[[Category: Savitsky, P]]
+[[Category: Thangaratnarajah C]]
-[[Category: Sharpe, T D]]
+[[Category: Ugochukwu E]]
-[[Category: Thangaratnarajah, C]]
+[[Category: Vollmar M]]
-[[Category: Ugochukwu, E]]
+[[Category: Weigelt J]]
-[[Category: Vollmar, M]]
+[[Category: Yue W]]
-[[Category: Weigelt, J]]
+[[Category: Zhang Y]]
-[[Category: Yue, W]]
+[[Category: Von Delft F]]
-[[Category: Zhang, Y]]
-[[Category: Indirubin]]
-[[Category: Kinase]]
-[[Category: Pctaire1]]
-[[Category: Sgc]]
-[[Category: Transferase]]

3mtl: Difference between revisions

Latest revision as of 11:06, 2 August 2023

Crystal structure of the PCTAIRE1 kinase in complex with Indirubin E804

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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