The making and breaking of symmetry in virus capsid assembly: glimpses of capsid biology from cryoelectron microscopy
The making and breaking of symmetry in virus capsid assembly: glimpses of capsid biology from cryoelectron microscopy
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病毒衣壳组装中对称性的形成和破坏：从冷冻电子显微镜观察衣壳生物学
DOI：
10.1096/fasebj.11.10.9271358
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
James F. Conway
中科院分区：
文献类型：
--
作者：
A. Steven;B. Trus;F. Booy;N. Cheng;A. Zlotnick;J. Castón;James F. Conway
病毒衣壳构成了一个多样化和通用的蛋白质结合容器和隔室家族，直径范围从约200 kDa（质量约1 MDa）到>1500 kDa（质量> 250 MDa）。衣壳的冷冻电子显微镜，现在达到分辨率低至10 μ m，揭示了新的结构基序，组装机制，和主要表位的精确位置。衣壳基本上是对称的结构，二十面体表面晶格已被证明是广泛的。然而，许多衣壳蛋白表现出显着的对称性破缺的倾向，从而在不同的晶格位点化学相同的亚基具有显着不同的结构和包装关系。给定亚基构象的时间差异也表现在伴随衣壳成熟的大规模构象变化中。更大和更复杂的衣壳，如DNA噬菌体和单纯疱疹病毒，不是通过简单的自组装形成的，而是在严格调控的程序的控制下形成的，这些程序可能包括病毒支架蛋白和细胞伴侣蛋白的参与，成熟的蛋白水解和史诗规模的构象变化。除了对病毒学的重要性外，衣壳相关研究还对一般生物学产生影响，涉及执行许多重要细胞功能的大分子复合物的组装过程。Steven，A. C.的方法，特鲁斯，B。L.，Booy，F. P.，Cheng，N.，兹洛特尼克，A.，卡斯顿，J.R.，康威，J.F.病毒衣壳装配中对称性的形成和破坏：从冷冻电子显微镜看衣壳生物学。FASEB J. 11，733-742（1997）
Virus capsids constitute a diverse and versatile family of protein‐bound containers and compartments ranging in diameter from ~200 Å (mass~1 MDa) to >1500 Å (mass> 250 MDa). Cryoelectron microscopy of capsids, now attaining resolutions down to 10 Å, is disclosing novel structural motifs, assembly mechanisms, and the precise locations of major epitopes. Capsids are essentially symmetric structures, and icosahedral surface lattices have proved to be widespread. However, many capsid proteins exhibit a remarkable propensity for symmetry breaking, whereby chemically identical subunits in distinct lattice sites have markedly different structures and packing relationships. Temporal differences in the conformation of a given subunit are also manifested in the large‐scale conformational changes that accompany capsid maturation. Larger and more complex capsids, such as DNA bacteriophages and herpes simplex virus, are formed not by simple self‐assembly, but under the control of tightly regulated programs that may include the involvement of viral scaffolding proteins and cellular chaperonins, maturational proteolysis, and conformational changes on an epic scale. In addition to its significance for virology, capsid‐related research has implications for biology in general, relating to the still largely obscure assembly processes of macromolecular complexes that perform many important cellular functions.—Steven, A. C., Trus, B. L., Booy, F. P., Cheng, N., Zlotnick, A., Caston, J. R., Conway, J. F. The making and breaking of symmetry in virus capsid assembly: glimpses of capsid biology from cryoelectron microscopy. FASEB J. 11, 733–742 (1997)
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影响因子：
3.4
作者：
BAKER, TS;NEWCOMB, WW;BROWN, JC
通讯作者：
BROWN, JC
DOI：
10.1172/jci115369
发表时间：
1991-09
期刊：
The Journal of clinical investigation
影响因子：
--
作者：
M. Nibert;Dierdre Furlong;B. Fields
通讯作者：
M. Nibert;Dierdre Furlong;B. Fields
影响因子：
2.9
作者：
R. Tuma;P. Prevelige;G. Thomas
通讯作者：
R. Tuma;P. Prevelige;G. Thomas
影响因子：
5.6
作者：
ThumanCommike, PA;Greene, B;Chiu, W
通讯作者：
Chiu, W
DOI：
10.1073/pnas.90.15.7015
发表时间：
1993-08-01
影响因子：
11.1
作者：
SMITH, TJ;OLSON, NH;BAKER, TS
通讯作者：
BAKER, TS