Hanson Sonya M, Sansom Mark S P, Becker Esther B E
†Molecular Physiology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, United States.
‡Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Biochemistry. 2015 Jul 7;54(26):4033-41. doi: 10.1021/acs.biochem.5b00235. Epub 2015 Jun 26.
A gain-of-function mutation (T635A) in the transient receptor potential (TRP) channel TRPC3 results in abnormal channel gating and causes cerebellar ataxia in the dominant Moonwalker (Mwk) mouse mutant. However, the underlying molecular and structural mechanisms are unclear. Here, we used a combined approach of computational modeling and functional characterization of proposed TRPC3 mutants. Our findings support a mechanism by which the hydrogen bonding capability of threonine 635 plays a significant role in maintaining a stable, closed state channel. This capability is lost in the Mwk mutant, suggesting a structural basis for the disease-causing phenotype in the Mwk mouse.
瞬时受体电位(TRP)通道TRPC3中的功能获得性突变(T635A)导致通道门控异常,并在显性“月球漫步者”(Mwk)小鼠突变体中引起小脑共济失调。然而,其潜在的分子和结构机制尚不清楚。在这里,我们使用了计算建模和对所提出的TRPC3突变体进行功能表征的联合方法。我们的研究结果支持了一种机制,即苏氨酸635的氢键结合能力在维持稳定的关闭状态通道中起重要作用。这种能力在Mwk突变体中丧失,这表明了Mwk小鼠致病表型的结构基础。