1AK4

HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID

Summary for 1AK4

• Entry DOI: 10.2210/pdb1ak4/pdb
• Descriptor: CYCLOPHILIN A, HIV-1 CAPSID (3 entities in total)
• Functional Keywords: capsid, hiv-1, cyclophilin a, isomerase, rotamase complex (capsid protein-cyclosporin), viral protein-isomerase complex, viral protein/isomerase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P62937; Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• Total number of polymer chains: 4
• Total formula weight: 68308.00

Authors

Hill, C.P.,Gamble, T.R.,Vajdos, F.F.,Worthylake, D.K.,Sundquist, W.I. (deposition date: 1997-05-28, release date: 1997-10-15, Last modification date: 2024-05-22)

Primary citation

Gamble, T.R.,Vajdos, F.F.,Yoo, S.,Worthylake, D.K.,Houseweart, M.,Sundquist, W.I.,Hill, C.P.
Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid.
Cell(Cambridge,Mass.), 87:1285-1294, 1996

PubMed Abstract: The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.

PubMed: 8980234
DOI: 10.1016/S0092-8674(00)81823-1

Experimental method

X-RAY DIFFRACTION (2.36 Å)