Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A-Reference-Cited by-同舟云学术

Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A

Published:2020-08-03 Issue:9 Volume:27 Page:855-862
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Ni Tao^ORCID,Gerard Samuel^ORCID,Zhao Gongpu^ORCID,Dent Kyle,Ning Jiying,Zhou Jing,Shi Jiong,Anderson-Daniels Jordan,Li Wen,Jang Sooin,Engelman Alan N.,Aiken Christopher,Zhang Peijun^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

https://www.nature.com/articles/s41594-020-0467-8.pdf

Reference57 articles.

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2. Li, Y.-L. et al. Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids. Elife 5, 582 (2016).

3. Smaga, S. S. et al. MxB restricts HIV-1 by targeting the tri-hexamer interface of the viral capsid. Structure 27, 1234–1245 (2019).

4. Gres, A. T. et al. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability. Science 349, 99–103 (2015).

5. Pornillos, O. et al. X-ray structures of the hexameric building block of the HIV capsid. Cell 137, 1282–1292 (2009).

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