1ak4: Difference between revisions
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Revision as of 16:52, 12 November 2007
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HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID
OverviewOverview
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.
About this StructureAbout this Structure
1AK4 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid., Gamble TR, Vajdos FF, Yoo S, Worthylake DK, Houseweart M, Sundquist WI, Hill CP, Cell. 1996 Dec 27;87(7):1285-94. PMID:8980234
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