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< | ==CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (UNLIGANDED FORM)== | ||
<StructureSection load='2jfm' size='340' side='right'caption='[[2jfm]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jfm]] 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=2JFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JFM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></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=2jfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfm OCA], [https://pdbe.org/2jfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfm RCSB], [https://www.ebi.ac.uk/pdbsum/2jfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfm ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/2jfm_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=2jfm ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation of these sites have not been elucidated. Here, we report on three novel and diverse protein kinase structures that reveal an exchanged activation segment conformation. This dimeric arrangement results in an active kinase conformation in trans, with activation segment phosphorylation sites in close proximity to the active site of the interacting protomer. Analytical ultracentrifugation and chemical cross-linking confirmed the presence of dimers in solution. Consensus substrate sequences for each kinase showed that the identified activation segment autophosphorylation sites are non-consensus substrate sites. Based on the presented structural and functional data, a model for specific activation segment phosphorylation at non-consensus substrate sites is proposed that is likely to be common to other kinases from diverse subfamilies. | |||
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.,Pike AC, Rellos P, Niesen FH, Turnbull A, Oliver AW, Parker SA, Turk BE, Pearl LH, Knapp S EMBO J. 2008 Feb 20;27(4):704-14. Epub 2008 Jan 31. PMID:18239682<ref>PMID:18239682</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jfm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith CH]] | |||
[[Category: Arrowsmith | [[Category: Bunkoczi G]] | ||
[[Category: Bunkoczi | [[Category: Edwards A]] | ||
[[Category: Fedorov O]] | |||
[[Category: Edwards | [[Category: Keates T]] | ||
[[Category: Fedorov | [[Category: Knapp S]] | ||
[[Category: Keates | [[Category: Papagrigoriou E]] | ||
[[Category: Knapp | [[Category: Pike ACW]] | ||
[[Category: Papagrigoriou | [[Category: Rellos P]] | ||
[[Category: Pike | [[Category: Salah E]] | ||
[[Category: Rellos | [[Category: Savitsky P]] | ||
[[Category: Salah | [[Category: Sundstrom M]] | ||
[[Category: Savitsky | [[Category: Weigelt J]] | ||
[[Category: Sundstrom | [[Category: Von Delft F]] | ||
[[Category: Weigelt | |||
[[Category: | |||
Latest revision as of 04:05, 21 November 2024
CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (UNLIGANDED FORM)CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (UNLIGANDED FORM)
Structural highlights
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 PubMedProtein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation of these sites have not been elucidated. Here, we report on three novel and diverse protein kinase structures that reveal an exchanged activation segment conformation. This dimeric arrangement results in an active kinase conformation in trans, with activation segment phosphorylation sites in close proximity to the active site of the interacting protomer. Analytical ultracentrifugation and chemical cross-linking confirmed the presence of dimers in solution. Consensus substrate sequences for each kinase showed that the identified activation segment autophosphorylation sites are non-consensus substrate sites. Based on the presented structural and functional data, a model for specific activation segment phosphorylation at non-consensus substrate sites is proposed that is likely to be common to other kinases from diverse subfamilies. Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.,Pike AC, Rellos P, Niesen FH, Turnbull A, Oliver AW, Parker SA, Turk BE, Pearl LH, Knapp S EMBO J. 2008 Feb 20;27(4):704-14. Epub 2008 Jan 31. PMID:18239682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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