title: The positively charged residues in the fragment 71 - 77 of complexin is required for its binding to SNARE complex.
abstract: Complexin is a cytoplasmic protein that plays an important role in the neurotransmitters release triggered by action potential. Previous studies suggested that complexin performs its functions through interaction with the SNARE complex. The crystal structure of complexin/SNARE complex revealed that complexin binds to SNARE core complex in an anti-parallel conformation with its residues 48 - 70. However, the functions of the flanking sequences are unclear. In this paper, we demonstrate that the fragment 71 - 77 of complexin is indispensable for its binding to the SNARE complex. Moreover, this interaction can be impaired by abolishing the positive charges in the fragment 71 - 77, which suggests that the positive charges in the fragment 71 - 77 are important for the interaction between complexin II and the SNARE complex.
authors: Department of Biological Sciences and Biotechnology, State-Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing, China.
authors: Jingguo
authors: J
authors: Liu
authors: Yong
authors: Y
authors: Wei
authors: Ting
authors: T
authors: Guo
authors: Xin
authors: X
authors: Xie
authors: Jiansen
authors: J
authors: Jiang
authors: Sen-fang
authors: SF
authors: Sui
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport; D000595:Amino Acid Sequence; D000818:Animals; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051381:Rats; D050600:SNARE Proteins / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; D009419:Nerve Tissue Proteins; D050600:SNARE Proteins; C095993:complexin II