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==Human EphA3 kinase and juxtamembrane region, Y596F mutant== | ==Human EphA3 kinase and juxtamembrane region, Y596F mutant== | ||
<StructureSection load='2qof' size='340' side='right' caption='[[2qof]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='2qof' size='340' side='right'caption='[[2qof]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qof]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2qof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QOF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gsf|2gsf]], [[2qo2|2qo2]], [[2qo7|2qo7]], [[2qo9|2qo9]], [[2qob|2qob]], [[2qoc|2qoc]], [[2qod|2qod]], [[2qoi|2qoi]], [[2qok|2qok]], [[2qol|2qol]], [[2qon|2qon]], [[2qoo|2qoo]], [[2qoq|2qoq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gsf|2gsf]], [[2qo2|2qo2]], [[2qo7|2qo7]], [[2qo9|2qo9]], [[2qob|2qob]], [[2qoc|2qoc]], [[2qod|2qod]], [[2qoi|2qoi]], [[2qok|2qok]], [[2qol|2qol]], [[2qon|2qon]], [[2qoo|2qoo]], [[2qoq|2qoq]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPHA3 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPHA3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qof OCA], [https://pdbe.org/2qof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qof RCSB], [https://www.ebi.ac.uk/pdbsum/2qof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qof ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 14: | Line 14: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qof_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qof_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 29: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 2qof" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2qof" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ephrin receptor 3D structures|Ephrin receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 34: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 11:27, 25 June 2021
Human EphA3 kinase and juxtamembrane region, Y596F mutantHuman EphA3 kinase and juxtamembrane region, Y596F mutant
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 PubMedEphrin receptors (Eph) affect cell shape and movement, unlike other receptor tyrosine kinases that directly affect proliferative pathways. The kinase domain of EphA3 is activated by ephrin binding and receptor oligomerization. This activation is associated with two tyrosines in the juxtamembrane region; these tyrosines are sites of autophosphorylation and interact with the active site of the kinase to modulate activity. This allosteric event has important implications both in terms of understanding signal transduction pathways mediated by Eph kinases as well as discovering specific therapeutic ligands for receptor kinases. In order to provide further details of the molecular mechanism through which the unphosphorylated juxtamembrane region blocks catalysis, we studied wild-type and site-specific mutants in detail. High-resolution structures of multiple states of EphA3 kinase with and without the juxtamembrane segment allowed us to map the coupled pathway of residues that connect the juxtamembrane segment, the activation loop, and the catalytic residues of the kinase domain. This highly conserved set of residues likely delineates a molecular recognition pathway for most of the Eph RTKs, helping to characterize the dynamic nature of these physiologically important enzymes. Autoregulation by the juxtamembrane region of the human ephrin receptor tyrosine kinase A3 (EphA3).,Davis TL, Walker JR, Loppnau P, Butler-Cole C, Allali-Hassani A, Dhe-Paganon S Structure. 2008 Jun;16(6):873-84. PMID:18547520[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Large Structures
- Receptor protein-tyrosine kinase
- Arrowsmith, C H
- Bochkarev, A
- Butler-Cole, C
- Davis, T
- Dhe-Paganon, S
- Edwards, A M
- Mackenzie, F
- Newman, E M
- Structural genomic
- Sundstrom, M
- Walker, J R
- Weigelt, J
- Atp-binding
- Juxtamembrane segment
- Nucleotide-binding
- Phosphorylation
- Receptor tyrosine kinase
- Sgc
- Transferase
- Transmembrane
- Tyrosine-protein kinase