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Cryo-EM micrographs of HIV-1 Vif bound to human APOBEC3H, CBF-beta, ELOB, ELOC, CUL5, and RBX2

ABSTRACT:

SUBMITTER: Fumiaki Ito

PROVIDER: EMPIAR-11423 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3H.

Ito Fumiaki F Alvarez-Cabrera Ana L AL Kim Kyumin K Zhou Z Hong ZH Chen Xiaojiang S XS

Nature communications 20230828 1

Human APOBEC3 (A3) cytidine deaminases are antiviral factors that are particularly potent against retroviruses. As a countermeasure, HIV-1 uses a viral infectivity factor (Vif) to target specific human A3s for proteasomal degradation. Vif recruits cellular transcription cofactor CBF-β and Cullin-5 (CUL5) RING E3 ubiquitin ligase to bind different A3s distinctively, but how this is accomplished remains unclear in the absence of the atomic structure of the complex. Here, we present the cryo-EM str ...[more]

PMID: 37640699

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