2izx

<table><tr><td colspan='2'>[[2izx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IZX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2izx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izx OCA], [http://pdbe.org/2izx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2izx RCSB], [http://www.ebi.ac.uk/pdbsum/2izx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2izx ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/KAP2_HUMAN KAP2_HUMAN]] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.

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== Publication Abstract from PubMed ==

Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A kinase-anchoring proteins (AKAPs) restricts the action of this broad specificity kinase. The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA both in the apo state and in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition. AKAP-IS folds into an amphipathic alpha helix that engages an essentially preformed shallow groove on the surface of the RII dimer D/D domains. Conserved AKAP aliphatic residues dominate interactions to RII at the predominantly hydrophobic interface, whereas polar residues are important in conferring R subunit isoform specificity. Using a peptide screening approach, we have developed SuperAKAP-IS, a peptide that is 10,000-fold more selective for the RII isoform relative to RI and can be used to assess the impact of PKA isoform-selective anchoring on cAMP-responsive events inside cells.

Molecular basis of AKAP specificity for PKA regulatory subunits.,Gold MG, Lygren B, Dokurno P, Hoshi N, McConnachie G, Tasken K, Carlson CR, Scott JD, Barford D Mol Cell. 2006 Nov 3;24(3):383-95. PMID:17081989<ref>PMID:17081989</ref>

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

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<div class="pdbe-citations 2izx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: CAMP-dependent protein kinase]]

[[Category: Barford, D]]

[[Category: Carlson, C R]]

[[Category: Dokurno, P]]

[[Category: Gold, M G]]

[[Category: Hoshi, N]]

[[Category: Lygren, B]]

[[Category: McConnachie, G]]

[[Category: Scott, J D]]

[[Category: Tasken, K]]

[[Category: Transferase]]