Rhesus TRIM5α disrupts the HIV-1 capsid at the inter-hexamer interfaces.
TRIM proteins play important roles in the innate immune defense against retroviral infection, including human immunodeficiency virus type-1 (HIV-1). Rhesus macaque TRIM5α (TRIM5α(rh)) targets the HIV-1 capsid and blocks infection at an early post-entry stage, prior to reverse transcription. Studies...
Guardado en:
Autores principales: | Gongpu Zhao, Danxia Ke, Thomas Vu, Jinwoo Ahn, Vaibhav B Shah, Ruifeng Yang, Christopher Aiken, Lisa M Charlton, Angela M Gronenborn, Peijun Zhang |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2011
|
Materias: | |
Acceso en línea: | https://doaj.org/article/fdf7626b6bc34083ba2352640dadd6bb |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid.
por: Xin Meng, et al.
Publicado: (2012) -
In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature
por: Soumeya A. Jaballah, et al.
Publicado: (2017) -
Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site
por: Chuang Liu, et al.
Publicado: (2016) -
Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer
por: Martin Obr, et al.
Publicado: (2021) -
In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway
por: Jiying Ning, et al.
Publicado: (2016)