Structure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule Binding

The capsid (CA) protein plays crucial roles in HIV infection and replication, essential to viral maturation. The absence of high-resolution structural data on unassembled CA hinders the development of antivirals effective in inhibiting assembly. Unlike enzymes that have targetable, functional substr...

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Veröffentlicht in:	Journal of molecular biology 2011-02, Vol.406 (3), p.371-386
Hauptverfasser:	Du, Shoucheng, Betts, Laurie, Yang, Ruifeng, Shi, Haibin, Concel, Jason, Ahn, Jinwoo, Aiken, Christopher, Zhang, Peijun, Yeh, Joanne I.
Format:	Artikel
Sprache:	eng
Schlagworte:	adenosine diphosphate Allosteric properties alternative dimer states assembly inhibitor Binding Sites capsid Capsid protein Capsid Proteins Capsid Proteins - chemistry Capsid Proteins - metabolism Capsids chemistry coat proteins conformational trapping Crystal structure Crystallization Crystallography, X-Ray Crystals Data processing Drug development drugs Electron microscopy Enzymes gag Gene Products, Human Immunodeficiency Virus gag Gene Products, Human Immunodeficiency Virus - chemistry gag Gene Products, Human Immunodeficiency Virus - metabolism hinge-binding site HIV Infections HIV Infections - virology HIV-1 HIV-1 - chemistry HIV-1 - physiology Human immunodeficiency virus 1 Humans Infection metabolism Models, Molecular Molecular Structure native full-length HIV-1 capsid crystal structure physiology Protein Binding Protein Conformation Protein Structure, Tertiary Replication Trapping virology Virus Replication
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