View source for 6bku


==Crystal Structure of the Human CAMKK2B bound to GSK650394==
<StructureSection load='6bku' size='340' side='right' caption='[[6bku]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bku]] 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=6BKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BKU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DXV:2-cyclopentyl-4-(5-phenyl-1H-pyrrolo[2,3-b]pyridin-3-yl)benzoic+acid'>DXV</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMKK2, CAMKKB, KIAA0787 ([http://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'>[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=6bku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bku OCA], [http://pdbe.org/6bku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bku RCSB], [http://www.ebi.ac.uk/pdbsum/6bku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bku ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KKCC2_HUMAN KKCC2_HUMAN]] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.<ref>PMID:11395482</ref> <ref>PMID:12935886</ref> <ref>PMID:9662074</ref> <ref>PMID:21957496</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Calcium/calmodulin-dependent protein kinase]]
[[Category: Human]]
[[Category: Arruda, P]]
[[Category: Counago, R M]]
[[Category: Drewry, D]]
[[Category: Edwards, A M]]
[[Category: Elkins, J M]]
[[Category: Massirer, K B]]
[[Category: Ramos, P Z]]
[[Category: Reis, C V.dos]]
[[Category: Structural genomic]]
[[Category: Souza, G P.de]]
[[Category: Protein kinase domain]]
[[Category: Sgc]]
[[Category: Transferase]]
[[Category: Transferase inhibitor complex]]