| Autor: |
White, Mark A., Sheng Li, Tsalkova, Tamara, Mei, Fang C., Tong Liu, Woods Jr., Virgil L., Xiaodong Cheng |
| Předmět: |
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| Zdroj: |
PLoS ONE; Nov2012, Vol. 7 Issue 11, Special section p1-9, 9p |
| Abstrakt: |
Exchange proteins directly activated by cAMP (EPACs) are important allosteric regulators of cAMP-mediated signal transduction pathways. To understand the molecular mechanism of EPAC activation, we have combined site-directed mutagenesis, X-ray crystallography, and peptide amide hydrogen/deuterium exchange mass spectrometry (DXMS) to probe the structural and conformational dynamics of EPAC2-F435G, a constitutively active EPAC2 mutant. Our study demonstrates that conformational dynamics plays a critical role in cAMP-induced EPAC activation. A glycine mutation at 435 position shifts the equilibrium of conformational dynamics towards the extended active conformation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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