4fg9: Difference between revisions
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[[ | ==Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-320 in complex with ATP== | ||
<StructureSection load='4fg9' size='340' side='right' caption='[[4fg9]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fg9]] 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=4FG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FG9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fg7|4fg7]], [[4fg8|4fg8]], [[4fgb|4fgb]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </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=4fg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fg9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fg9 RCSB], [http://www.ebi.ac.uk/pdbsum/4fg9 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human calcium/calmodulin-dependent protein kinase I (CaMKI) plays pivotal roles in the nervous system. The activity of human CaMKI is regulated by a regulatory region including an autoinhibitory segment and a CaM-binding segment. We report here four structures of three CaMKIalpha truncates in apo form and in complexes with ATP. In an apo, autoinhibited structure, the activation segment adopts a unique helical conformation which together with the autoinhibitory segment constrains helices alphaC and alphaD in inactive conformations, sequesters Thr177 from being phosphorylated, and occludes the substrate-binding site. In an ATP-bound, inactive structure, the activation segment is largely disordered and the CaM-binding segment protrudes out ready for CaM binding. In an ATP-bound, active structure, the regulatory region is dissociated from the catalytic core and the catalytic site assumes an active conformation. Detailed structural analyses reveal the interplay of the regulatory region, the activation segment, and the nucleotide-binding site in the regulation of CaMKI. | |||
Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI.,Zha M, Zhong C, Ou Y, Han L, Wang J, Ding J PLoS One. 2012;7(9):e44828. doi: 10.1371/journal.pone.0044828. Epub 2012 Sep 20. PMID:23028635<ref>PMID:23028635</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Calcium/calmodulin-dependent protein kinase]] | [[Category: Calcium/calmodulin-dependent protein kinase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ding, J | [[Category: Ding, J]] | ||
[[Category: Han, L | [[Category: Han, L]] | ||
[[Category: Ou, Y | [[Category: Ou, Y]] | ||
[[Category: Wang, J | [[Category: Wang, J]] | ||
[[Category: Zha, M | [[Category: Zha, M]] | ||
[[Category: Zhong, C | [[Category: Zhong, C]] | ||
[[Category: Autoinhibition]] | [[Category: Autoinhibition]] | ||
[[Category: Calmodulin]] | [[Category: Calmodulin]] | ||
Revision as of 17:29, 4 January 2015
Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-320 in complex with ATPCrystal structure of human calcium/calmodulin-dependent protein kinase I 1-320 in complex with ATP
Structural highlights
Publication Abstract from PubMedHuman calcium/calmodulin-dependent protein kinase I (CaMKI) plays pivotal roles in the nervous system. The activity of human CaMKI is regulated by a regulatory region including an autoinhibitory segment and a CaM-binding segment. We report here four structures of three CaMKIalpha truncates in apo form and in complexes with ATP. In an apo, autoinhibited structure, the activation segment adopts a unique helical conformation which together with the autoinhibitory segment constrains helices alphaC and alphaD in inactive conformations, sequesters Thr177 from being phosphorylated, and occludes the substrate-binding site. In an ATP-bound, inactive structure, the activation segment is largely disordered and the CaM-binding segment protrudes out ready for CaM binding. In an ATP-bound, active structure, the regulatory region is dissociated from the catalytic core and the catalytic site assumes an active conformation. Detailed structural analyses reveal the interplay of the regulatory region, the activation segment, and the nucleotide-binding site in the regulation of CaMKI. Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI.,Zha M, Zhong C, Ou Y, Han L, Wang J, Ding J PLoS One. 2012;7(9):e44828. doi: 10.1371/journal.pone.0044828. Epub 2012 Sep 20. PMID:23028635[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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