1zxa: Difference between revisions
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[[ | ==Solution Structure of the Coiled-Coil Domain of cGMP-dependent Protein Kinase Ia== | ||
<StructureSection load='1zxa' size='340' side='right' caption='[[1zxa]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zxa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZXA FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRKG1, PRKGR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=1zxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zxa RCSB], [http://www.ebi.ac.uk/pdbsum/1zxa PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing structural and functional studies. However, owing to the dynamic nature of many of the smaller coiled-coil domains, crystallization for X-ray studies is very challenging. Determination of elongated structures using standard NMR approaches is inefficient and usually yields low-resolution structures due to accumulation of small errors over long distances. Here we describe a solution NMR approach based on residual dipolar couplings (RDCs) for rapid and accurate structure determination of coiled-coil dimers. Using this approach, we were able to determine the high-resolution structure of the coiled-coil domain of cGMP-dependent protein kinase Ialpha, a protein of previously unknown structure that is critical for physiological relaxation of vascular smooth muscle. This approach can be extended to solve coiled-coil structures with higher order assemblies. | |||
Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.,Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ Protein Sci. 2005 Sep;14(9):2421-8. PMID:16131665<ref>PMID:16131665</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
Revision as of 11:29, 8 October 2014
Solution Structure of the Coiled-Coil Domain of cGMP-dependent Protein Kinase IaSolution Structure of the Coiled-Coil Domain of cGMP-dependent Protein Kinase Ia
Structural highlights
Publication Abstract from PubMedCoiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing structural and functional studies. However, owing to the dynamic nature of many of the smaller coiled-coil domains, crystallization for X-ray studies is very challenging. Determination of elongated structures using standard NMR approaches is inefficient and usually yields low-resolution structures due to accumulation of small errors over long distances. Here we describe a solution NMR approach based on residual dipolar couplings (RDCs) for rapid and accurate structure determination of coiled-coil dimers. Using this approach, we were able to determine the high-resolution structure of the coiled-coil domain of cGMP-dependent protein kinase Ialpha, a protein of previously unknown structure that is critical for physiological relaxation of vascular smooth muscle. This approach can be extended to solve coiled-coil structures with higher order assemblies. Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.,Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ Protein Sci. 2005 Sep;14(9):2421-8. PMID:16131665[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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