通过主链 (13)CO-(15)N 旋转回波双共振固态 NMR 检测膜中闭合的流感病毒血凝素融合肽结构。
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
机构信息
Department of Chemistry, Michigan State University, 578 S. Shaw Lane, East Lansing, MI 48824, USA.
出版信息
J Biomol NMR. 2013 Feb;55(2):139-46. doi: 10.1007/s10858-013-9709-y. Epub 2013 Jan 18.
Abstract
The influenza virus fusion peptide is the N-terminal ~20 residues of the HA2 subunit of the hemagglutinin protein and this peptide plays a key role in the fusion of the viral and endosomal membranes during initial infection of a cell. The fusion peptide adopts N-helix/turn/C-helix structure in both detergent and membranes with reports of both open and closed interhelical topologies. In the present study, backbone (13)CO-(15)N REDOR solid-state NMR was applied to the membrane-associated fusion peptide to detect the distribution of interhelical distances. The data clearly showed a large fraction of closed and semi-closed topologies and were best-fitted to a mixture of two structures that do not exchange. One of the earlier open structural models may have incorrect G13 dihedral angles derived from TALOS analysis of experimentally correct (13)C shifts.
摘要
流感病毒融合肽是血凝素蛋白 HA2 亚基的 N 端~20 个残基，该肽段在病毒和内体膜融合过程中在细胞初始感染中发挥关键作用。融合肽在去污剂和膜中均采用 N-螺旋/转弯/C-螺旋结构，有报道称存在开放和闭合的螺旋拓扑结构。在本研究中，采用基于 backbone (13)CO-(15)N REDOR 的固态 NMR 技术对膜相关融合肽进行检测，以探测螺旋间距离的分布。数据清楚地显示了大量的闭合和半闭合拓扑结构，与不发生交换的两种结构的混合物拟合最好。较早的一种开放结构模型可能存在不正确的 G13 二面角，这是由实验上正确的 (13)C 位移的 TALOS 分析得出的。
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