4qxk
From Proteopedia
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| - | ''' | + | ==Joint X-ray/neutron structure of PKGIbeta in complex with cGMP== |
| + | <StructureSection load='4qxk' size='340' side='right' caption='[[4qxk]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qxk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QXK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.12 2.7.11.12] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qxk RCSB], [http://www.ebi.ac.uk/pdbsum/4qxk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | High selectivity of cyclic-nucleotide binding (CNB) domains for cAMP and cGMP are required for segregating signaling pathways; however, the mechanism of selectivity remains unclear. To investigate the mechanism of high selectivity in cGMP-dependent protein kinase (PKG), we determined a room-temperature joint X-ray/neutron (XN) structure of PKG Ibeta CNB-B, a domain 200-fold selective for cGMP over cAMP, bound to cGMP (2.2 A), and a low-temperature X-ray structure of CNB-B with cAMP (1.3 A). The XN structure directly describes the hydrogen bonding interactions that modulate high selectivity for cGMP, while the structure with cAMP reveals that all these contacts are disrupted, explaining its low affinity for cAMP. | ||
| - | + | Neutron Diffraction Reveals Hydrogen Bonds Critical for cGMP-Selective Activation: Insights for cGMP-Dependent Protein Kinase Agonist Design.,Huang GY, Gerlits OO, Blakeley MP, Sankaran B, Kovalevsky AY, Kim C Biochemistry. 2014 Nov 4;53(43):6725-7. doi: 10.1021/bi501012v. Epub 2014 Oct 22. PMID:25271401<ref>PMID:25271401</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Gerlits, O]] | ||
| + | [[Category: Huang, G Y]] | ||
| + | [[Category: Kim, C]] | ||
| + | [[Category: Kovalevsky, A]] | ||
| + | [[Category: Cyclic nucleotide selectivity]] | ||
| + | [[Category: Hydrogen bonding]] | ||
| + | [[Category: Second messenger]] | ||
| + | [[Category: Serine/threonine protein kinase]] | ||
| + | [[Category: Signal transduction]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Solvent accessibility]] | ||
Revision as of 06:56, 12 November 2014
Joint X-ray/neutron structure of PKGIbeta in complex with cGMP
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