2izy: Difference between revisions
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<StructureSection load='2izy' size='340' side='right'caption='[[2izy]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2izy' size='340' side='right'caption='[[2izy]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2izy]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2izy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZY FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2izy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izy OCA], [https://pdbe.org/2izy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2izy RCSB], [https://www.ebi.ac.uk/pdbsum/2izy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2izy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/KAP2_MOUSE KAP2_MOUSE] 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Barford D]] | |||
[[Category: Barford | [[Category: Carlson CR]] | ||
[[Category: Carlson | [[Category: Dokurno P]] | ||
[[Category: Dokurno | [[Category: Gold MG]] | ||
[[Category: Gold | [[Category: Hoshi N]] | ||
[[Category: Hoshi | [[Category: Lygren B]] | ||
[[Category: Lygren | [[Category: McConnachie G]] | ||
[[Category: McConnachie | [[Category: Scott JD]] | ||
[[Category: Scott | [[Category: Tasken K]] | ||
[[Category: Tasken | |||
Latest revision as of 12:32, 9 May 2024
Molecular Basis of AKAP Specificity for PKA Regulatory SubunitsMolecular Basis of AKAP Specificity for PKA Regulatory Subunits
Structural highlights
FunctionKAP2_MOUSE 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLocalization 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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