Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B

Holger Rehmann (), Ernesto Arias-Palomo, Michael A. Hadders, Frank Schwede, Oscar Llorca and Johannes L. Bos
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Holger Rehmann: Centre for Biomedical Genetics and Cancer Genomics Centre, University Medical Center, Universiteitsweg 100
Ernesto Arias-Palomo: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain
Michael A. Hadders: Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands
Frank Schwede: BIOLOG Life Science Institute, Flughafendamm 9a, 28199 Bremen, Germany
Oscar Llorca: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain
Johannes L. Bos: Centre for Biomedical Genetics and Cancer Genomics Centre, University Medical Center, Universiteitsweg 100

Nature, 2008, vol. 455, issue 7209, 124-127

Abstract: Epac proteins: changes on cyclic AMP binding Epac proteins are activated by binding of cyclic AMP (cAMP) and act as guanine nucleotide exchange factors for Rap GTPases. They are important in the regulation of cell adhesion and insulin secretion. Here, the structure of Epac2 in a complex with cAMP and Rap1B is determined. Comparison of this activated state of the complex with the inactive one reveals the conformational changes in Epac2 induced by cAMP binding.

Date: 2008
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DOI: 10.1038/nature07187

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