CALCIUM-CHANNEL ACTIVITY OF PURIFIED HUMAN SYNEXIN AND STRUCTURE OF THE HUMAN SYNEXIN GENE
CALCIUM-CHANNEL ACTIVITY OF PURIFIED HUMAN SYNEXIN AND STRUCTURE OF THE HUMAN SYNEXIN GENE
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DOI：
10.1073/pnas.86.10.3798
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发表时间：
1989-05-01
影响因子：
11.1
通讯作者：
POLLARD, HB
中科院分区：
文献类型：
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作者：
BURNS, AL;MAGENDZO, K;POLLARD, HB
Synexin是一种钙依赖性膜结合蛋白，不仅融合膜，而且作为电压依赖性钙通道。我们已经分离和测序了一组重叠的cDNA克隆的人synexin。突触蛋白的衍生氨基酸序列揭示了与先前鉴定的一类钙依赖性膜结合蛋白在C-末端结构域中的强同源性。这些包括内切蛋白II、脂皮质素I、钙调蛋白I重链（p36）、蛋白II和钙电蛋白67 K。Mr 51，000的突触蛋白分子可分为一个独特的，高度疏水的167个氨基酸的N-末端结构域和一个保守的299个氨基酸的C-末端区域。后者结构域由交替的疏水和亲水片段组成。对整个结构的分析揭示了可能的见解，如电压敏感性钙通道活性，离子选择性，对磷脂的亲和力和膜融合等不同的性质。
Synexin is a calcium-dependent membrane binding protein that not only fuses membranes but also acts as a voltage-dependent calcium channel. We have isolated and sequenced a set of overlapping cDNA clones for human synexin. The derived amino acid sequence of synexin reveals strong homology in the C-terminal domain with a previously identified class of calcium-dependent membrane binding proteins. These include endonexin II, lipocortin I, calpactin I heavy chain (p36), protein II, and calelectrin 67K. The Mr 51,000 synexin molecule can be divided into a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Analysis of the entire structure reveals possible insights such diverse properties as voltage-sensitive calcium channel activity, ion selectivity, affinity for phospholipids, and membrane fusion.