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2lru
From Proteopedia
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| - | + | ==Solution Structure of the WNK1 Autoinhibitory Domain== | |
| - | + | <StructureSection load='2lru' size='340' side='right' caption='[[2lru]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lru]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LRU FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Wnk1, Hsn2, Prkwnk1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=2lru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lru OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lru RCSB], [http://www.ebi.ac.uk/pdbsum/2lru PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | WNK1 [with no lysine (K)-1] is a 250-kDa serine/threonine protein kinase involved in the maintenance of cellular salt levels and is directly linked to a hereditary form of hypertension. Here, we report the solution NMR structure of the autoinhibitory domain of WNK1 (WNK1-AI), a small regulatory subunit that lies immediately C-terminal of the kinase domain. We show that this domain is a homolog of the RFXV-binding PASK/FRAY homology 2 (PF2) domain found in OSR (oxidative stress responsive kinase) and SPAK (serine/threonine proline-alanine-rich kinase) kinases, which are substrates of WNK1. The WNK1-AI has a circularly permuted topology relative to the OSR1-PF2 domain. Nevertheless, like PF2 domains, WNK1-AI binds peptides that contain an RFXV motif with micromolar affinities as assessed by changes in (1)H,(15)N heteronuclear single quantum coherence spectra. Mutations to the WNK1-AI and binding peptides confirm a similar binding mode. | ||
| - | + | Solution Structure of the WNK1 Autoinhibitory Domain, a WNK-Specific PF2 Domain.,Moon TM, Correa F, Kinch LN, Piala AT, Gardner KH, Goldsmith EJ J Mol Biol. 2013 Jan 30. pii: S0022-2836(13)00047-8. doi:, 10.1016/j.jmb.2013.01.031. PMID:23376100<ref>PMID:23376100</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | <references | + | *[[Serine/threonine protein kinase|Serine/threonine protein kinase]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Correa, F | + | [[Category: Correa, F]] |
| - | [[Category: Gardner, K H | + | [[Category: Gardner, K H]] |
| - | [[Category: Goldsmith, E J | + | [[Category: Goldsmith, E J]] |
| - | [[Category: Moon, T M | + | [[Category: Moon, T M]] |
[[Category: Autoinhibitory domain]] | [[Category: Autoinhibitory domain]] | ||
[[Category: Pf2 domain]] | [[Category: Pf2 domain]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 12:19, 18 December 2014
Solution Structure of the WNK1 Autoinhibitory Domain
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