3kl8

From Proteopedia

(Difference between revisions)

Revision as of 21:48, 24 December 2014

CaMKIINtide Inhibitor Complex

Structural highlights

3kl8 is a 10 chain structure with sequence from Caenorhabditis elegans and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3kk8, 3kk9
Gene:	unc-43, K11E8.1, K11E8.1d (Caenorhabditis elegans), Camk2n1 (Rattus norvegicus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q9U6Q0_CAEEL] Role in locomotion and neuronal cell fate specification. Required for the regulation of synaptic density, egg laying, defecation, and meiotic maturation. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.^[1] ^[2] ^[3] ^[4]

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 PubMed

The dodecameric holoenzyme of calcium-calmodulin-dependent protein kinase II (CaMKII) responds to high-frequency Ca(2+) pulses to become Ca(2+) independent. A simple coincidence-detector model for Ca(2+)-frequency dependency assumes noncooperative activation of kinase domains. We show that activation of CaMKII by Ca(2+)-calmodulin is cooperative, with a Hill coefficient of approximately 3.0, implying sequential kinase-domain activation beyond dimeric units. We present data for a model in which cooperative activation includes the intersubunit 'capture' of regulatory segments. Such a capture interaction is seen in a crystal structure that shows extensive contacts between the regulatory segment of one kinase and the catalytic domain of another. These interactions are mimicked by a natural inhibitor of CaMKII. Our results show that a simple coincidence-detection model cannot be operative and point to the importance of kinetic dissection of the frequency-response mechanism in future experiments.

Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation.,Chao LH, Pellicena P, Deindl S, Barclay LA, Schulman H, Kuriyan J Nat Struct Mol Biol. 2010 Mar;17(3):264-72. Epub 2010 Feb 7. PMID:20139983^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Solomon A, Bandhakavi S, Jabbar S, Shah R, Beitel GJ, Morimoto RI. Caenorhabditis elegans OSR-1 regulates behavioral and physiological responses to hyperosmotic environments. Genetics. 2004 May;167(1):161-70. PMID:15166144
↑ Umemura T, Rapp P, Rongo C. The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking. J Cell Sci. 2005 Aug 1;118(Pt 15):3327-38. PMID:16079277 doi:10.1242/jcs.02457
↑ Liu Q, Chen B, Ge Q, Wang ZW. Presynaptic Ca2+/calmodulin-dependent protein kinase II modulates neurotransmitter release by activating BK channels at Caenorhabditis elegans neuromuscular junction. J Neurosci. 2007 Sep 26;27(39):10404-13. PMID:17898212 doi:10.1523/JNEUROSCI.5634-06.2007
↑ Nehrke K, Denton J, Mowrey W. Intestinal Ca2+ wave dynamics in freely moving C. elegans coordinate execution of a rhythmic motor program. Am J Physiol Cell Physiol. 2008 Jan;294(1):C333-44. Epub 2007 Oct 17. PMID:17942636 doi:10.1152/ajpcell.00303.2007
↑ Chao LH, Pellicena P, Deindl S, Barclay LA, Schulman H, Kuriyan J. Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation. Nat Struct Mol Biol. 2010 Mar;17(3):264-72. Epub 2010 Feb 7. PMID:20139983 doi:10.1038/nsmb.1751

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kl8"

@@ Line 7: / Line 7: @@
 <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=3kl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3kl8 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q9U6Q0_CAEEL Q9U6Q0_CAEEL]] Role in locomotion and neuronal cell fate specification. Required for the regulation of synaptic density, egg laying, defecation, and meiotic maturation. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.<ref>PMID:15166144</ref> <ref>PMID:16079277</ref> <ref>PMID:17898212</ref> <ref>PMID:17942636</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3kl8

From Proteopedia

Revision as of 21:48, 24 December 2014

CaMKIINtide Inhibitor Complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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