NDLI: Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site

Content Provider	PubMed Central
Author	Liu, Chuang Perilla, Juan R. Ning, Jiying Lu, Manman Hou, Guangjin Ramalho, Ruben Himes, Benjamin A. Zhao, Gongpu Bedwell, Gregory J. Byeon, In-ja Ahn, Jinwoo Gronenborn, Angela M. Prevelige, Peter E. Rousso, Itay Aiken, Christopher Polenova, Tatyana Schulten, Klaus Zhang, Peijun
Copyright Year	2016
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.
Related Links	http://dx.doi.org/10.1038/ncomms10714
Starting Page	10714
File Format	PDF
ISSN	20411723
e-ISSN	20411723
Journal	Nature Communications
Volume Number	7
Language	English
Publisher	Nature Publishing Group
Publisher Date	2016-03-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Physics and Astronomy(all) Chemistry(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Physics and Astronomy Biochemistry, Genetics and Molecular Biology

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3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site

Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies

Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase

Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein.

Allostery through the computational microscope: cAMP activation of a canonical signaling domain

Maturation of the HIV-1 core by a non-diffusional phase transition

Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site

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Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site

Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.

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Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase

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Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site