2R83

Crystal structure analysis of human synaptotagmin 1 C2A-C2B

2R83 の概要

• エントリーDOI: 10.2210/pdb2r83/pdb
• 分子名称: Synaptotagmin-1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: c2a-c2b, exocytosis, calcium, cell junction, cytoplasmic vesicle, glycoprotein, lipoprotein, membrane, metal-binding, palmitate, phosphorylation, synapse, transmembrane, endocytosis-exocytosis complex, endocytosis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass membrane protein : P21579
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65352.56

構造登録者

Sutton, R.B.,Fuson, K.L.,Montes, M.,Robert, J.J. (登録日: 2007-09-10, 公開日: 2008-02-12, 最終更新日: 2023-08-30)

主引用文献

Fuson, K.L.,Montes, M.,Robert, J.J.,Sutton, R.B.
Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association.
Biochemistry, 46:13041-13048, 2007

PubMed Abstract: Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them.

PubMed: 17956130
DOI: 10.1021/bi701651k

実験手法

X-RAY DIFFRACTION (2.7 Å)