1o7f

<table><tr><td colspan='2'>[[1o7f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7F FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7f OCA], [https://pdbe.org/1o7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7f RCSB], [https://www.ebi.ac.uk/pdbsum/1o7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7f ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Cyclic adenosine monophosphate (cAMP) is a universal second messenger that, in eukaryotes, was believed to act only on cAMP-dependent protein kinase A (PKA) and cyclic nucleotide-regulated ion channels. Recently, guanine nucleotide exchange factors specific for the small GTP-binding proteins Rap1 and Rap2 (Epacs) were described, which are also activated directly by cAMP. Here, we have determined the three-dimensional structure of the regulatory domain of Epac2, which consists of two cyclic nucleotide monophosphate (cNMP)-binding domains and one DEP (Dishevelled, Egl, Pleckstrin) domain. This is the first structure of a cNMP-binding domain in the absence of ligand, and comparison with previous structures, sequence alignment and biochemical experiments allow us to delineate a mechanism for cyclic nucleotide-mediated conformational change and activation that is most likely conserved for all cNMP-regulated proteins. We identify a hinge region that couples cAMP binding to a conformational change of the C-terminal regions. Mutations in the hinge of Epac can uncouple cAMP binding from its exchange activity.

Structure and regulation of the cAMP-binding domains of Epac2.,Rehmann H, Prakash B, Wolf E, Rueppel A, de Rooij J, Bos JL, Wittinghofer A Nat Struct Biol. 2003 Jan;10(1):26-32. PMID:12469113<ref>PMID:12469113</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1o7f" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Bos, J L]]

[[Category: Prakash, B]]

[[Category: Rehmann, H]]

[[Category: Rooij, J De]]

[[Category: Rueppel, A]]

[[Category: Wittinghofer, A]]

[[Category: Wolf, E]]

[[Category: Regulation]]