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首页> 外文期刊>Neuron >Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding.
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Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding.

机译:GABARAP的结构有两种构象:对GABA(A)受体定位和微管蛋白结合的影响。

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摘要

GABARAP recognizes and binds the gamma2 subunit of the GABA(A) receptor, interacts with microtubules and the N-ethyl maleimide sensitive factor, and is proposed to function in GABA(A) receptor trafficking and postsynaptic localization. We have determined the crystal structure of human GABARAP at 1.6 A resolution. The structure comprises an N-terminal helical subdomain and a ubiquitin-like C-terminal domain. Structure-based mutational analysis demonstrates that the N-terminal subdomain is responsible for tubulin binding while the C-terminal domain contains the binding site for the GABA(A). A second GABARAP crystal form was determined at 1.9 A resolution and documents that GABARAP can self-associate in a head-to-tail manner. The structural details of this oligomerization reveal how GABARAP can both promote tubulin polymerization and facilitate GABA(A) receptor clustering.
机译:GABARAP识别并结合GABA(A)受体的gamma2亚基,与微管和N-乙基马来酰亚胺敏感因子相互作用,并被提议在GABA(A)受体运输和突触后定位中发挥作用。我们确定了1.6 A分辨率的人GABARAP的晶体结构。该结构包括N端螺旋亚结构域和泛素样C端结构域。基于结构的突变分析表明,N末端亚结构域负责微管蛋白结合,而C末端结构域包含GABA(A)的结合位点。第二个GABARAP晶型是在1.9 A分辨率下确定的,并记录了GABARAP可以从头到尾的方式自缔合。这种低聚的结构细节揭示了GABARAP如何既促进微管蛋白聚合又促进GABA(A)受体聚类。

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