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Solution structure of the WNK1 autoinhibitory domain, a WNK-specific PF2 domain.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Moon TM,Correa F,Kinch LN,Piala AT,Gardner KH,Goldsmith EJ

doi

10.1016/j.jmb.2013.01.031

subject

Has Abstract

pub_date

2013-04-26 00:00:00

pages

1245-52

issue

8

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(13)00047-8

journal_volume

425

pub_type

杂志文章

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