A SPRING-LOADED MECHANISM FOR THE CONFORMATIONAL CHANGE OF INFLUENZA HEMAGGLUTININ
A SPRING-LOADED MECHANISM FOR THE CONFORMATIONAL CHANGE OF INFLUENZA HEMAGGLUTININ
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DOI：
10.1016/0092-8674(93)90260-w
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发表时间：
1993-05-21
期刊：
影响因子：
64.5
通讯作者：
KIM, PS
中科院分区：
文献类型：
--
作者：
CARR, CM;KIM, PS
流感病毒血凝素（HA）经历构象变化，诱导病毒与细胞膜融合。HA在融合状态下的结构是未知的。我们已经确定了HA中的一个序列，该序列具有形成卷曲螺旋的高倾向。令人惊讶的是，该序列对应于天然HA的X射线结构中的环区域：该环后面是三链卷曲螺旋茎。我们发现，一个36个残基的肽（LOOP-36），包括环区和茎的第一部分，形成一个三链卷曲螺旋。该卷曲的科尔被延伸并稳定在较长的肽中，对应于LOOP-36加上前面的短α螺旋的残基。这些发现导致了HA的融合构象的模型：天然状态的卷曲螺旋茎延伸，将疏水融合肽向靶膜重新定位100埃。
Influenza hemagglutinin (HA) undergoes a conformational change that induces viral fusion with the cellular membrane. The structure of HA in the fusogenic state is unknown. We have identified a sequence in HA that has a high propensity for forming a coiled coil. Surprisingly, this sequence corresponds to a loop region in the X-ray structure of native HA: the loop is followed by a three-stranded, coiled-coil stem. We find that a 36 residue peptide (LOOP-36), comprising the loop region and the first part of the stem, forms a three-stranded coiled coil. This coiled coll is extended and stabilized in a longer peptide, corresponding to LOOP-36 plus the residues of a preceding, short alpha helix. These findings lead to a model for the fusogenic conformation of HA: the coiled-coil stem of the native state extends, relocating the hydrophobic fusion peptide, by 100 angstrom, toward the target membrane.