STRUCTURE OF THE FIRST C-2 DOMAIN OF SYNAPTOTAGMIN .1. A NOVEL CA2+/PHOSPHOLIPID-BINDING FOLD
STRUCTURE OF THE FIRST C-2 DOMAIN OF SYNAPTOTAGMIN .1. A NOVEL CA2+/PHOSPHOLIPID-BINDING FOLD
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DOI：
10.1016/0092-8674(95)90296-1
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发表时间：
1995-03-24
期刊：
影响因子：
64.5
通讯作者：
SPRANG, SR
中科院分区：
文献类型：
--
作者：
SUTTON, RB;DAVLETOV, BA;SPRANG, SR
C-2结构域是自然界中广泛存在的调控序列基序。突触结合蛋白I是一种参与胞吐的Ca 2+调节的突触囊泡蛋白，包含两个C-2结构域，其中第一个结构域充当Ca 2+传感器。我们现在以1.9埃的分辨率描述该C-2结构域在Ca 2+结合和Ca 2+游离形式下的三维结构。C-2多肽形成围绕被指定为C-2键的保守四链基序构建的八链β夹心。Ca 2+结合在位于C-2-关键基序的N-和C-末端的两个多肽环之间的杯状凹陷中。
C-2 domains are regulatory sequence motifs that occur widely in nature. Synaptotagmin I, a synaptic vesicle protein involved in the Ca2+ regulation of exocytosis, contains two C-2 domains, the first of which acts as a Ca2+ sensor. We now describe the three-dimensional structure of this C-2 domain at 1.9 Angstrom resolution in both the Ca2+-bound and Ca2+-free forms. The C-2 polypeptide forms an eight-stranded beta sandwich constructed around a conserved four-stranded motif designated as a C-2 key. Ca2+ binds in a cup-shaped depression between two polypeptide loops located at the N- and C-termini of the C-2-key motif.