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High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus.

Acta Crystallogr F Struct Biol Commun. 2015 Aug;71(Pt 8):1088-93. Epub 2015 Jul 29
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摘要


Protein kinases (PKs) are dynamic regulators of numerous cellular processes. Their phosphorylation activity is determined by the conserved kinase core structure, which is maintained by the interaction and dynamics with associated domains or interacting proteins. The prototype enzyme for investigations to understand the activity and regulation of PKs is the catalytic subunit of cAMP-dependent protein kinase Major effects of functional regulation and ligand binding are driven by only minor structural modulations in protein-protein interactions. In order to resolve such minor structural differences, very high resolution structures are required. Here, the high-resolution X-ray structure of from Cricetulus griseus is reported.

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基因功能


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原始数据


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