1cdm

<table><tr><td colspan='2'>[[1cdm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CDM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1cdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cdm OCA], [http://pdbe.org/1cdm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cdm RCSB], [http://www.ebi.ac.uk/pdbsum/1cdm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cdm ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). [[http://www.uniprot.org/uniprot/KCC2A_RAT KCC2A_RAT]] CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity.<ref>PMID:15312654</ref>

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== Publication Abstract from PubMed ==

Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase II alpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.

Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures.,Meador WE, Means AR, Quiocho FA Science. 1993 Dec 10;262(5140):1718-21. PMID:8259515<ref>PMID:8259515</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Meador, W E]]

[[Category: Quiocho, F A]]

[[Category: Calcium-binding protein]]