Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into HIV-1 polyanion-dependent capsid lattice formation revealed by single particle cryo-EM.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 120, Issue 18, Page e2220545120, Year 2023
Publish date	May 2, 2023
Authors	Carolyn M Highland / Aaron Tan / Clifton L Ricaña / John A G Briggs / Robert A Dick /
PubMed Abstract	The HIV-1 capsid houses the viral genome and interacts extensively with host cell proteins throughout the viral life cycle. It is composed of capsid protein (CA), which assembles into a conical ...The HIV-1 capsid houses the viral genome and interacts extensively with host cell proteins throughout the viral life cycle. It is composed of capsid protein (CA), which assembles into a conical fullerene lattice composed of roughly 200 CA hexamers and 12 CA pentamers. Previous structural analyses of individual CA hexamers and pentamers have provided valuable insight into capsid structure and function, but detailed structural information about these assemblies in the broader context of the capsid lattice is lacking. In this study, we combined cryoelectron tomography and single particle analysis (SPA) cryoelectron microscopy to determine structures of continuous regions of the capsid lattice containing both hexamers and pentamers. We also developed a method of liposome scaffold-based in vitro lattice assembly ("lattice templating") that enabled us to directly study the lattice under a wider range of conditions than has previously been possible. Using this approach, we identified a critical role for inositol hexakisphosphate in pentamer formation and determined the structure of the CA lattice bound to the capsid-targeting antiretroviral drug GS-6207 (lenacapavir). Our work reveals key structural details of the mature HIV-1 CA lattice and establishes the combination of lattice templating and SPA as a robust strategy for studying retroviral capsid structure and capsid interactions with host proteins and antiviral compounds.
External links	Proc Natl Acad Sci U S A / PubMed:37094124 / PubMed Central
Methods	EM (subtomogram averaging) / EM (single particle)
Resolution	3.1 - 7.1 Å
Structure data	EMDB-16698: Subtomogram average of HIV-1 CA pentamer from capsid-like particles assembled with inositol hexakisphosphate Method: EM (subtomogram averaging) / Resolution: 6.2 Å EMDB-16699: Subtomogram average of HIV-1 CA hexamer from capsid-like particles assembled with inositol hexakisphosphate Method: EM (subtomogram averaging) / Resolution: 3.9 Å 29772 8g6k EMDB-29772, PDB-8g6k: HIV-1 CA lattice bound to IP6; from capsid-like particles Method: EM (single particle) / Resolution: 3.6 Å 29773 8g6l EMDB-29773, PDB-8g6l: HIV-1 capsid lattice bound to IP6, pH 6.2 Method: EM (single particle) / Resolution: 3.3 Å 29774 8g6m EMDB-29774, PDB-8g6m: HIV-1 CA lattice bound to IP6, pH 7.4 Method: EM (single particle) / Resolution: 3.1 Å 29775 8g6n EMDB-29775, PDB-8g6n: HIV-1 capsid lattice bound to dNTPs Method: EM (single particle) / Resolution: 3.5 Å 29776 8g6o EMDB-29776, PDB-8g6o: HIV-1 capsid lattice bound to IP6 and Lenacapavir Method: EM (single particle) / Resolution: 3.1 Å EMDB-29777: Defective HIV-1 CA pentamer in surrounding hexameric lattice Method: EM (single particle) / Resolution: 7.1 Å
Source	Escherichia coli (E. coli) human immunodeficiency virus 1
Keywords	VIRUS LIKE PARTICLE / HIV-1 / capsid / lattice / virus