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首页> 外文期刊>Neuron >Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1.
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Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1.

机译：ClC-1中抑制剂结合位点揭示了氯离子通道结构的保守性。

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摘要

Crystal structures of bacterial CLC proteins were solved recently, but it is unclear to which level of detail they can be extrapolated to mammalian chloride channels. Exploiting the difference in inhibition by 9-anthracene carboxylic acid (9-AC) between ClC-0, -1, and -2, we identified a serine between helices O and P as crucial for 9-AC binding. Mutagenesis based on the crystal structure identified further residues affecting inhibitor binding. They surround a partially hydrophobic pocket close to the chloride binding site that is accessible from the cytoplasm, consistent with the observed intracellular block by 9-AC. Mutations in presumably Cl--coordinating residues yield additional insights into the structure and function of ClC-1. Our work shows that the structure of bacterial CLCs can be extrapolated with fidelity to mammalian Cl- channels.
机译：细菌CLC蛋白的晶体结构最近得到了解决，但是尚不清楚它们可以推断到哺乳动物氯化物通道的详细程度。利用ClC-0，-1和-2之间的9-蒽羧酸（9-AC）抑制作用的差异，我们确定了螺旋O和P之间的丝氨酸对于9-AC结合至关重要。基于晶体结构的诱变确定了影响抑制剂结合的其他残基。它们围绕着从细胞质可接近的氯化物结合位点的部分疏水性口袋，这与通过9-AC观察到的细胞内阻滞相一致。推测为Cl-配位残基的突变可进一步了解ClC-1的结构和功能。我们的工作表明，细菌CLC的结构可以精确地推断到哺乳动物C1通道。

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