6bq8

<StructureSection load='6bq8' size='340' side='right' caption='[[6bq8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[6bq8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BQ8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6FW:2-AMINO-8-[(4-CHLOROPHENYL)SULFANYL]-9-[(2S,4AR,6R,7R,7AS)-2,7-DIHYDROXY-2-OXOTETRAHYDRO-2H,4H-2LAMBDA~5~-FURO[3,2-D][1,3,2]DIOXAPHOSPHININ-6-YL]-3,9-DIHYDRO-6H-PURIN-6-ONE'>6FW</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</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=6bq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bq8 OCA], [http://pdbe.org/6bq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bq8 RCSB], [http://www.ebi.ac.uk/pdbsum/6bq8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bq8 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

As one of the main receptors of a second messenger, cGMP, cGMP-dependent protein kinase (PKG) isoforms I and II regulate distinct physiological processes. The design of isoform-specific activators is thus of great biomedical importance and requires detailed structural information about PKG isoforms bound with activators, including accurate positions of hydrogen atoms and a description of the hydrogen bonding and water architecture. Here, we determined a 2.2 A room-temperature joint X-ray/neutron (XN) structure of the human PKG II carboxyl cyclic nucleotide binding (CNB-B) domain bound with a potent PKG II activator, 8-pCPT-cGMP. The XN structure directly visualizes intermolecular interactions and reveals changes in hydrogen bonding patterns upon comparison to the X-ray structure determined at cryo-temperatures. Comparative analysis of the backbone hydrogen/deuterium exchange patterns in PKG II:8-pCPT-cGMP and previously reported PKG Ibeta:cGMP XN structures suggests that the ability of these agonists to activate PKG is related to how effectively they quench dynamics of the cyclic nucleotide binding pocket and the surrounding regions.

 

Neutron Crystallography Detects Differences in Protein Dynamics: Structure of the PKG II Cyclic Nucleotide Binding Domain in Complex with an Activator.,Gerlits O, Campbell JC, Blakeley MP, Kim C, Kovalevsky A Biochemistry. 2018 Mar 13. doi: 10.1021/acs.biochem.8b00010. PMID:29517905<ref>PMID:29517905</ref>

 

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

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<references/>

[[Category: Transferase]]

[[Category: Gerlits, O]]

[[Category: Kim, C]]

[[Category: Kovalevsky, A]]

[[Category: Activator]]

[[Category: Signaling protein]]