2x0g: Difference between revisions
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[[Image: | ==X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX== | ||
<StructureSection load='2x0g' size='340' side='right' caption='[[2x0g]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X0G FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f3z|2f3z]], [[1j7p|1j7p]], [[1nkf|1nkf]], [[1k93|1k93]], [[1xfv|1xfv]], [[1sk6|1sk6]], [[1y6w|1y6w]], [[1iwq|1iwq]], [[1jkl|1jkl]], [[1k90|1k90]], [[1yrt|1yrt]], [[1cll|1cll]], [[1lvc|1lvc]], [[2w73|2w73]], [[1cdl|1cdl]], [[1jkt|1jkt]], [[1xfy|1xfy]], [[1xfu|1xfu]], [[2f3y|2f3y]], [[1xfx|1xfx]], [[1jks|1jks]], [[1s26|1s26]], [[1j7o|1j7o]], [[1ctr|1ctr]], [[1jkk|1jkk]], [[2w4j|2w4j]], [[2w4k|2w4k]], [[1yru|1yru]], [[1wrz|1wrz]], [[2wel|2wel]], [[2v02|2v02]], [[1xfz|1xfz]], [[1p4f|1p4f]], [[1pk0|1pk0]], [[2v01|2v01]], [[1xfw|1xfw]], [[2be6|2be6]], [[1ig1|1ig1]], [[1zot|1zot]], [[1sw8|1sw8]], [[2vay|2vay]], [[1aji|1aji]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x0g RCSB], [http://www.ebi.ac.uk/pdbsum/2x0g PDBsum]</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/x0/2x0g_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Death-associated protein kinase (DAPK) provides a model for calcium-bound calmodulin (CaM)-dependent protein kinases (CaMKs). Here, we report the crystal structure of the binary DAPK-CaM complex, using a construct that includes the DAPK catalytic domain and adjacent autoregulatory domain. When DAPK was in a complex with CaM, the DAPK autoregulatory domain formed a long seven-turn helix. This DAPK-CaM module interacted with the DAPK catalytic domain through two separate domain-domain interfaces, which involved the upper and the lower lobe of the catalytic domain. When bound to DAPK, CaM adopted an extended conformation, which was different from that in CaM-CaMK peptide complexes. Complementary biochemical analysis showed that the ability of DAPK to bind CaM correlated with its catalytic activity. Because many features of CaM binding are conserved in other CaMKs, our findings likely provide a generally applicable model for regulation of CaMK activity. | |||
Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex.,de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M Sci Signal. 2010 Jan 26;3(106):ra6. PMID:20103772<ref>PMID:20103772</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Calmodulin|Calmodulin]] | *[[Calmodulin|Calmodulin]] | ||
*[[Death-associated protein kinase|Death-associated protein kinase]] | *[[Death-associated protein kinase|Death-associated protein kinase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] |