2vag

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:12, 13 December 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
==CRYSTAL STRUCTURE OF DI-PHOSPHORYLATED HUMAN CLK1 IN COMPLEX WITH A NOVEL SUBSTITUTED INDOLE INHIBITOR==
+
 
-
<StructureSection load='2vag' size='340' side='right' caption='[[2vag]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
==Crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole inhibitor==
 +
<StructureSection load='2vag' size='340' side='right'caption='[[2vag]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2vag]] 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=2VAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VAG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2vag]] 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=2VAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VAG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=V25:ETHYL+3-[(E)-2-AMINO-1-CYANOETHENYL]-6,7-DICHLORO-1-METHYL-1H-INDOLE-2-CARBOXYLATE'>V25</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]] 1.8&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>, <scene name='pdbligand=V25:ETHYL+3-[(E)-2-AMINO-1-CYANOETHENYL]-6,7-DICHLORO-1-METHYL-1H-INDOLE-2-CARBOXYLATE'>V25</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z57|1z57]]</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=2vag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vag OCA], [https://pdbe.org/2vag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vag RCSB], [https://www.ebi.ac.uk/pdbsum/2vag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vag ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dual-specificity_kinase Dual-specificity kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.12.1 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=2vag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vag OCA], [http://pdbe.org/2vag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vag RCSB], [http://www.ebi.ac.uk/pdbsum/2vag PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/CLK1_HUMAN CLK1_HUMAN]] Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.<ref>PMID:10480872</ref> <ref>PMID:19168442</ref>
+
[https://www.uniprot.org/uniprot/CLK1_HUMAN CLK1_HUMAN] Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.<ref>PMID:10480872</ref> <ref>PMID:19168442</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vag_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vag_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
Line 32: Line 31:
==See Also==
==See Also==
-
*[[Dual specificity protein kinase|Dual specificity protein kinase]]
+
*[[Dual specificity protein kinase 3D structures|Dual specificity protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Dual-specificity kinase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
-
[[Category: Arrowsmith, C H]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Bracher, F]]
+
[[Category: Bracher F]]
-
[[Category: Bullock, A N]]
+
[[Category: Bullock AN]]
-
[[Category: Delft, F Von]]
+
[[Category: Edwards A]]
-
[[Category: Edwards, A]]
+
[[Category: Fedorov O]]
-
[[Category: Fedorov, O]]
+
[[Category: Huber K]]
-
[[Category: Huber, K]]
+
[[Category: Knapp S]]
-
[[Category: Knapp, S]]
+
[[Category: Pike ACW]]
-
[[Category: Pike, A C.W]]
+
[[Category: Pilka ES]]
-
[[Category: Pilka, E S]]
+
[[Category: Sundstrom M]]
-
[[Category: Sundstrom, M]]
+
[[Category: Ugochukwu E]]
-
[[Category: Ugochukwu, E]]
+
[[Category: Weigelt J]]
-
[[Category: Weigelt, J]]
+
[[Category: Von Delft F]]
-
[[Category: Nucleus]]
+
-
[[Category: Serine/threonine-protein kinase]]
+
-
[[Category: Transferase]]
+
-
[[Category: Tyrosine-protein kinase]]
+

Current revision

Crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole inhibitor

PDB ID 2vag

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vag"
Personal tools