Solution Structure of a Double Mutant of the Carboxy-Terminal Dimerization Domain of the HIV-1 Capsid Protein†,‡

Biochemistry ◽  
2008 ◽  
Vol 47 (8) ◽  
pp. 2289-2297 ◽  
Author(s):  
Hing C. Wong ◽  
Ronald Shin ◽  
N. Rama Krishna
Keyword(s):  
Capsid Protein ◽  
Solution Structure ◽  
Double Mutant ◽  
Dimerization Domain ◽  
Carboxy Terminal ◽  
Hiv 1

scholarly journals An extensive thermodynamic characterization of the dimerization domain of the HIV-1 capsid protein

2005 ◽  
Vol 14 (9) ◽  
pp. 2387-2404 ◽  
Author(s):  
María C. Lidón-Moya ◽  
Francisco N. Barrera ◽  
Marta Bueno ◽  
Raúl Pérez-Jiménez ◽  
Javier Sancho ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Dimerization Domain ◽  
Thermodynamic Characterization ◽  
Hiv 1

scholarly journals Mutational Analysis and Allosteric Effects in the HIV-1 Capsid Protein Carboxyl-Terminal Dimerization Domain

2009 ◽  
Vol 10 (2) ◽  
pp. 390-399 ◽  
Author(s):  
Xiang Yu ◽  
Qiuming Wang ◽  
Jui-Chen Yang ◽  
Idit Buch ◽  
Chung-Jung Tsai ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Mutational Analysis ◽  
Dimerization Domain ◽  
Carboxyl Terminal ◽  
Hiv 1

scholarly journals The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: A biophysical characterization

2004 ◽  
Vol 13 (6) ◽  
pp. 1512-1523 ◽  
Author(s):  
María T. Garzón ◽  
María C. Lidón-Moya ◽  
Francisco N. Barrera ◽  
Alicia Prieto ◽  
Javier Gómez ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Dimerization Domain ◽  
Biophysical Characterization ◽  
Hiv 1

Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution

1999 ◽  
Vol 55 (1) ◽  
pp. 85-92 ◽  
Author(s):  
David K. Worthylake ◽  
Hui Wang ◽  
Sanghee Yoo ◽  
Wesley I. Sundquist ◽  
Christopher P. Hill
Keyword(s):  
Capsid Protein ◽  
Dimerization Domain ◽  
Protein Dimerization ◽  
Hiv 1

scholarly journals Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein

2007 ◽  
Vol 93 (4) ◽  
pp. 1264-1276 ◽  
Author(s):  
Luis A. Alcaraz ◽  
Marta del Álamo ◽  
Francisco N. Barrera ◽  
Mauricio G. Mateu ◽  
José L. Neira
Keyword(s):  
Capsid Protein ◽  
Solution Structure ◽  
Terminal Domain ◽  
Hiv 1

scholarly journals Insight into the HIV-1 Vif SOCS-box–ElonginBC interaction

Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  
Keyword(s):  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Dynamic Information ◽  
Ubiquitin Ligase Complex ◽  
Biophysical Studies ◽  
Viral Infectivity Factor ◽  
Β Sheet ◽  
Socs Box ◽  
Insight Into ◽  
Hiv 1

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

scholarly journals Structure, Function, and Interactions of the HIV-1 Capsid Protein

Life ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 100
Author(s):  
Eric Rossi ◽  
Megan E. Meuser ◽  
Camille J. Cunanan ◽  
Simon Cocklin
Keyword(s):  
Life Cycle ◽  
Capsid Protein ◽  
Adaptor Proteins ◽  
Restriction Factors ◽  
Gag Polyprotein ◽  
Immunodeficiency Virus ◽  
Host Cell Factors ◽  
Hiv 1

The capsid (CA) protein of the human immunodeficiency virus type 1 (HIV-1) is an essential structural component of a virion and facilitates many crucial life cycle steps through interactions with host cell factors. Capsid shields the reverse transcription complex from restriction factors while it enables trafficking to the nucleus by hijacking various adaptor proteins, such as FEZ1 and BICD2. In addition, the capsid facilitates the import and localization of the viral complex in the nucleus through interaction with NUP153, NUP358, TNPO3, and CPSF-6. In the later stages of the HIV-1 life cycle, CA plays an essential role in the maturation step as a constituent of the Gag polyprotein. In the final phase of maturation, Gag is cleaved, and CA is released, allowing for the assembly of CA into a fullerene cone, known as the capsid core. The fullerene cone consists of ~250 CA hexamers and 12 CA pentamers and encloses the viral genome and other essential viral proteins for the next round of infection. As research continues to elucidate the role of CA in the HIV-1 life cycle and the importance of the capsid protein becomes more apparent, CA displays potential as a therapeutic target for the development of HIV-1 inhibitors.

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