2LRU

Solution Structure of the WNK1 Autoinhibitory Domain

Summary for 2LRU

• Entry DOI: 10.2210/pdb2lru/pdb
• NMR Information: BMRB: 18398
• Descriptor: Serine/threonine-protein kinase WNK1 (1 entity in total)
• Functional Keywords: autoinhibitory domain, pf2 domain, transferase
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Cellular location: Cytoplasm: Q9JIH7
• Total number of polymer chains: 1
• Total formula weight: 11358.88

Authors

Moon, T.M.,Correa, F.,Gardner, K.H.,Goldsmith, E.J. (deposition date: 2012-04-13, release date: 2012-05-23, Last modification date: 2024-05-15)

Primary citation

Moon, T.M.,Correa, F.,Kinch, L.N.,Piala, A.T.,Gardner, K.H.,Goldsmith, E.J.
Solution Structure of the WNK1 Autoinhibitory Domain, a WNK-Specific PF2 Domain.
J.Mol.Biol., 425:1245-1252, 2013

PubMed Abstract: 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) and SPAK (serine/threonine proline-alanine-rich) 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.

PubMed: 23376100
DOI: 10.1016/j.jmb.2013.01.031

Experimental method

SOLUTION NMR