期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 23, 期 2, 页码 292-301出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2013.04.002
关键词
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资金
- Jane Coffin Childs Postdoctoral Fellowship
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM101277] Funding Source: NIH RePORTER
Ca2+/calmodulin dependent protein kinase II (CaMKII) is a broadly distributed metazoan Ser/Thr protein kinase that is important in neuronal and cardiac signaling. CaMKII forms oligomeric assemblies, typically dodecameric, in which the calcium-responsive kinase domains are organized around a central hub. We review the results of crystallographic analyses of CaMKII, including the recently determined structure of a full-length and autoinhibited form of the holoenzyme. These structures, when combined with other data, allow informed speculation about how CaMKII escapes calcium-dependence when calcium spikes exceed threshold frequencies.
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