Springs and hinges: dynamic coiled coils and discontinuities.
Springs and hinges: dynamic coiled coils and discontinuities.
复制标题
弹簧和铰链：动态盘绕线圈和不连续性。
DOI：
10.1016/0968-0004(94)90030-2
复制
发表时间：
1994
影响因子：
13.8
通讯作者：
Endow,SA
中科院分区：
文献类型：
--
作者：
Oas,TG;Endow,SA
卷曲螺旋不连续性在蛋白质功能中的可能作用。卷曲螺旋中的不连续性可能有助于蛋白质的功能，顶部：引起固定的弯曲，中间：提供灵活性，或底部：形成不同稳定性的亚结构域之间的边界，或稳定的卷曲螺旋和另一种结构的区域之间的边界。螺旋线圈用扭杆表示，螺旋线圈用粗线表示。螺旋的螺距近似于比例。机制s将血凝素-100 A的融合区从蛋白质中的埋藏位置置换到暴露的融合活性位置。与其他病毒融合蛋白的血凝素序列的比较表明，血凝素的构象变化方面的建议可能是共同的许多病毒包膜蛋白，包括1型人类免疫缺陷病毒（HIV-1）。最近用对应于包膜蛋白gp 41的38个残基的肽进行的实验表明，它形成卷曲螺旋，并且引人注目的是，该肽在体外有效地抑制gp 41介导的病毒-细胞和细胞-细胞融合14。这些结果表明，肽竞争与完整的gp 41卷曲螺旋形成与细胞表面蛋白。
Possible roles of coiled-coil discontinuities in protein function. Discontinuities in a coiled coil may contribute to protein function by top: causing fixed bends, middle: providing flexibility, or bottom: forming boundaries between subdomains of differing stability, or between stable coiled coils and regions of another structure. Coiled coil is depicted by twisted bars and t~ on. coiled coil by thick lines. The pitch of the (xhelices is approximately to scale. mechanism s, would displace the fusion region of hemagglutinin-I00 A from a buried position in the protein to an exposed, fusion-competent position. Comparison of the hemagglutinin sequence with those of other viral fusion proteins indicates that aspects of the conformational change propose l for hemagglutinin might be common to many viral envelope proteins, including that of the type 1 human immunodeficiency virus (HIV-I). Recent experiments with a 38-residue peptide corresponding to the envelope protein gp41, indicate that it forms a coiled coil and, strikingly, the peptide potently inhibits gp41-mediated virus-cell and cell-cell fusion in vitro 14. These results suggest that the peptide competes with intact gp41 for coiled-coil formation with cellsurface proteins.