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cAMP-dependent allostery and dynamics in Epac: an...
Journal article

cAMP-dependent allostery and dynamics in Epac: an NMR view

Abstract

Epac (exchange protein directly activated by cAMP) is a critical cAMP receptor, which senses cAMP and couples the cAMP signal to the catalysis of guanine exchange in the Rap substrate. In the present paper, we review the NMR studies that we have undertaken on the CBD (cyclic-nucleotide-binding domain) of Epac1. Our NMR investigations have shown that cAMP controls distal autoinhibitory interactions through long-range modulations in dynamics. …

Authors

Selvaratnam R; Akimoto M; VanSchouwen B; Melacini G

Journal

Biochemical Society Transactions, Vol. 40, No. 1, pp. 219–223

Publisher

Portland Press

Publication Date

February 1, 2012

DOI

10.1042/bst20110628

ISSN

0300-5127