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5FJB

Cyclophilin A Stabilize HIV-1 Capsid through a Novel Non- canonical Binding Site

Summary for 5FJB
Entry DOI10.2210/pdb5fjb/pdb
EMDB information3076
DescriptorGAG POLYPROTEIN, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A (2 entities in total)
Functional Keywordsisomerase
Biological sourceHUMAN IMMUNODEFICIENCY VIRUS 1
More
Cellular locationGag polyprotein: Host cell membrane ; Lipid-anchor . Matrix protein p17: Virion membrane ; Lipid-anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion : P03347
Cytoplasm : P62937
Total number of polymer chains3
Total formula weight66597.13
Authors
Primary citationLiu, C.,Perilla, J.R.,Ning, J.,Lu, M.,Hou, G.,Ramalho, R.,Himes, B.A.,Zhao, G.,Bedwell, G.J.,Byeon, I.,Ahn, J.,Gronenborn, A.M.,Prevelige, P.E.,Rousso, I.,Aiken, C.,Polenova, T.,Schulten, K.,Zhang, P.
Cyclophilin a Stabilizes the HIV-1 Capsid Through a Novel Non-Canonical Binding Site.
Nat.Commun., 7:10714-, 2016
Cited by
PubMed Abstract: The host cell factor cyclophilin A (CypA) interacts directly with the HIV-1 capsid and regulates viral infectivity. Although the crystal structure of CypA in complex with the N-terminal domain of the HIV-1 capsid protein (CA) has been known for nearly two decades, how CypA interacts with the viral capsid and modulates HIV-1 infectivity remains unclear. We determined the cryoEM structure of CypA in complex with the assembled HIV-1 capsid at 8-Å resolution. The structure exhibits a distinct CypA-binding pattern in which CypA selectively bridges the two CA hexamers along the direction of highest curvature. EM-guided all-atom molecular dynamics simulations and solid-state NMR further reveal that the CypA-binding pattern is achieved by single-CypA molecules simultaneously interacting with two CA subunits, in different hexamers, through a previously uncharacterized non-canonical interface. These results provide new insights into how CypA stabilizes the HIV-1 capsid and is recruited to facilitate HIV-1 infection.
PubMed: 26940118
DOI: 10.1038/NCOMMS10714
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (9 Å)
Structure validation

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