4LQW: Crystal Structure Of Hiv-1 Capsid N-terminal Domain In Complex With Nup358 Cyclophilin

Citation:
Abstract
BACKGROUND: 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. RESULTS: Here we present the crystal structure of the N-terminal capsid domain of HIV-1 in complex with the cyclophilin domain of nuclear pore protein NUP358. The structure reveals that HIV-1 is positioned to allow single-bond resonance stabilisation of exposed capsid residue P90. NMR exchange experiments demonstrate that NUP358 is an active isomerase, which efficiently catalyzes cis-trans isomerization of the HIV-1 capsid. In contrast, the distantly related feline lentivirus FIV can bind NUP358 but is neither isomerized by it nor requires it for infection. CONCLUSION: Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating.
PDB ID: 4LQWDownload
MMDB ID: 112681
PDB Deposition Date: 2013/7/19
Updated in MMDB: 2013/08
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)
Similar Structures:
Biological Unit for 4LQW: dimeric; determined by author
Molecular Components in 4LQW
Label Count Molecule
Proteins (2 molecules)
1
E3 Sumo-protein Ligase Ranbp2(Gene symbol: RANBP2)
Molecule annotation
1
Capsid Protein P24
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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