1cm4
From Proteopedia
(Difference between revisions)
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- | [[Image:1cm4.png|left|200px]] | ||
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{{STRUCTURE_1cm4| PDB=1cm4 | SCENE= }} | {{STRUCTURE_1cm4| PDB=1cm4 | SCENE= }} | ||
+ | ===Motions of calmodulin-four-conformer refinement=== | ||
+ | {{ABSTRACT_PUBMED_9438860}} | ||
- | === | + | ==Function== |
- | + | [[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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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:009438860</ref><references group="xtra"/> | + | <ref group="xtra">PMID:009438860</ref><references group="xtra"/><references/> |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Calcium/calmodulin-dependent protein kinase]] | [[Category: Calcium/calmodulin-dependent protein kinase]] | ||
[[Category: Phillips, G N.]] | [[Category: Phillips, G N.]] | ||
[[Category: Wall, M E.]] | [[Category: Wall, M E.]] | ||
+ | [[Category: Calcium-binding-transferase complex]] | ||
[[Category: Ef-hand calcium-binding protein]] | [[Category: Ef-hand calcium-binding protein]] |
Revision as of 11:19, 24 July 2013
Contents |
Motions of calmodulin-four-conformer refinement
Template:ABSTRACT PUBMED 9438860
Function
[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.[1]
About this Structure
1cm4 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
See Also
Reference
- Wall ME, Clarage JB, Phillips GN. Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering. Structure. 1997 Dec 15;5(12):1599-612. PMID:9438860
- ↑ Krapivinsky G, Medina I, Krapivinsky L, Gapon S, Clapham DE. SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation. Neuron. 2004 Aug 19;43(4):563-74. PMID:15312654 doi:10.1016/j.neuron.2004.08.003