4LQW

Crystal structure of HIV-1 capsid N-terminal domain in complex with NUP358 cyclophilin

Summary for 4LQW

Entry DOI	10.2210/pdb4lqw/pdb
Descriptor	E3 SUMO-protein ligase RanBP2, Capsid protein p24 (3 entities in total)
Functional Keywords	cyclophilin, isomerase, capsid
Biological source	Homo sapiens (human) More
Cellular location	Nucleus: P49792 Matrix protein p17: Virion . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P12497
Total number of polymer chains	4
Total formula weight	71835.79
Authors	Price, A.J.,James, L.C. (deposition date: 2013-07-19, release date: 2013-08-14, Last modification date: 2023-09-20)
Primary citation	Bichel, K.,Price, A.J.,Schaller, T.,Towers, G.J.,Freund, S.M.,James, L.C. HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358. Retrovirology, 10:81-81, 2013 Cited by PubMed Abstract: Lentiviruses such as HIV-1 can be distinguished from other retroviruses by the cyclophilin A-binding loop in their capsid and their ability to infect non-dividing cells. Infection of non-dividing cells requires transport through the nuclear pore but how this is mediated is unknown. PubMed: 23902822 DOI: 10.1186/1742-4690-10-81 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation