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The prolyl isomerase cyclophilin A (CypA) is required for efficient HIV-1 replication and is incorporated into virions through a binding interaction at the Gly-Pro 222 bond located within the capsid domain of the HIV-1 Gag precursor polyprotein (Pr gag ). It has recently been shown that CypA efficiently catalyzes the cis/trans isomerization of Gly-Pro 222 within the isolated N-terminal domain of capsid (CA N ). To address the proposal that CypA interacts with Gly-Pro sequences in the C-terminaldoi:10.1021/bi049841z pmid:15147195 fatcat:llng4tcx6vajvl7hwoz4wla7ru