4F7Z

Conformational dynamics of exchange protein directly activated by cAMP

Summary for 4F7Z

• Entry DOI: 10.2210/pdb4f7z/pdb
• Descriptor: Rap guanine nucleotide exchange factor 4, GLYCEROL (3 entities in total)
• Functional Keywords: cyclic nucleotide, gef, exchange factor, regulation, auto-inhibition, cdc25 homology domain, exocytosis
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm: Q9EQZ6
• Total number of polymer chains: 1
• Total formula weight: 114705.10

Authors

White, M.A.,Tsalkova, T.N.,Mei, F.C.,Liu, T.,Woods, V.L.,Cheng, X. (deposition date: 2012-05-16, release date: 2012-10-03, Last modification date: 2023-09-13)

Primary citation

White, M.A.,Li, S.,Tsalkova, T.,Mei, F.C.,Liu, T.,Woods, V.L.,Cheng, X.
Structural analyses of a constitutively active mutant of exchange protein directly activated by cAMP.
Plos One, 7:e49932-e49932, 2012

PubMed Abstract: 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.

PubMed: 23189173
DOI: 10.1371/journal.pone.0049932

Experimental method

X-RAY DIFFRACTION (2.6 Å)