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Structure and insights into the function of a Ca~(2+)-activated Cl~- channel

机译：Ca〜（2+）激活Cl〜-通道功能的结构和洞察力

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摘要

在本期Nature上发表的两篇论文中，作者发布了两个由Ca~（2+）激发的氯化物通道的X-射线晶体结构，它们是这种类型通道的首次发表的结构。Janine Brunner等人使“脂质混杂酶”发生了结晶，这种酶是催化脂质在一个双层的两叶之间运动的一种膜蛋白。该结构显示了一个亲水性跨膜空腔，该空腔暴露于脂质双层，催化过程可能在那里发生。Veronica Dickson等人使“bestrophin-1”发生了结晶。这个家族的蛋白会响应于细胞内Ca~(2+)浓度的上升将它们的阴离子选择性小孔打开。该结构显示，Ca~(2+)结合到一个五聚跨膜通道的胞质区域；并且还显示，该小孔是95A长，有至少15个不同的阴离子结合点。%Bestrophin calcium- activated chloride channels (CaCCs) regulate the flow of chloride and other monovalent anions across cellular membranes in response to intracellular calcium (Ca~(2+)) levels. Mutations in bestrophin 1 (BEST1) cause certain eye diseases. Here we present X-ray structures of chicken BEST1-Fab complexes, at 2.85 A resolution, with permeant anions and Ca~(2+). Representing, to our knowledge, the first structure of a CaCC, the eukaryotic BEST1 channel, which recapitulates CaCC function in liposomes, is formed from a pentameric assembly of subunits. Ca~(2+) binds to the channel's large cytosolic region. A single ion pore, approximately 95 A in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-π interactions. Conformational changes observed near the 'Ca~(2+) clasp, hint at the mechanism of Ca~(2+)-dependent gating. Disease-causing mutations are prevalent within the gating apparatus.
机译：在本期Nature上发表的两篇论文中，作者发布了两个由Ca~（2+）激发的氯化物通道的X-射线晶体结构，它们是这种类型通道的首次发表的结构。Janine Brunner等人使“脂质混杂酶”发生了结晶，这种酶是催化脂质在一个双层的两叶之间运动的一种膜蛋白。该结构显示了一个亲水性跨膜空腔，该空腔暴露于脂质双层，催化过程可能在那里发生。Veronica Dickson等人使“bestrophin-1”发生了结晶。这个家族的蛋白会响应于细胞内Ca~(2+)浓度的上升将它们的阴离子选择性小孔打开。该结构显示，Ca~(2+)结合到一个五聚跨膜通道的胞质区域；并且还显示，该小孔是95A长，有至少15个不同的阴离子结合点。%Bestrophin calcium- activated chloride channels (CaCCs) regulate the flow of chloride and other monovalent anions across cellular membranes in response to intracellular calcium (Ca~(2+)) levels. Mutations in bestrophin 1 (BEST1) cause certain eye diseases. Here we present X-ray structures of chicken BEST1-Fab complexes, at 2.85 A resolution, with permeant anions and Ca~(2+). Representing, to our knowledge, the first structure of a CaCC, the eukaryotic BEST1 channel, which recapitulates CaCC function in liposomes, is formed from a pentameric assembly of subunits. Ca~(2+) binds to the channel's large cytosolic region. A single ion pore, approximately 95 A in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-π interactions. Conformational changes observed near the 'Ca~(2+) clasp, hint at the mechanism of Ca~(2+)-dependent gating. Disease-causing mutations are prevalent within the gating apparatus.

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  • 来源
    《Nature》 |2014年第7530期|213-218a2|共7页
  • 作者

    Veronica Kane Dickson; Leanne Pedi; Stephen B. Long;

  • 作者单位

    Structural Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10065, USA;

    Structural Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10065, USA;

    Structural Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10065, USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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  • 正文语种 eng
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