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- W2056832018 abstract "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−Pro222 bond located within the capsid domain of the HIV-1 Gag precursor polyprotein (Prgag). It has recently been shown that CypA efficiently catalyzes the cis/trans isomerization of Gly−Pro222 within the isolated N-terminal domain of capsid (CAN). To address the proposal that CypA interacts with Gly−Pro sequences in the C-terminal domain of a mature capsid, the interaction between CypA and the natively folded, full-length capsid protein (CAFL) has been investigated here using nuclear magnetic resonance spectroscopy. In addition, a fragment of the Prgag protein encoding the full-matrix protein and the N-terminal domain of capsid (MA-CAN) has been used to probe the catalytic interaction between CypA and an immature form of the capsid. The results discussed herein strongly suggest that Gly−Pro222 located within the N-terminal domain of the capsid is the preferential site for CypA binding and catalysis and that catalysis of Gly−Pro222 is unaffected by maturational processing at the N-terminus of the capsid." @default.
- W2056832018 created "2016-06-24" @default.
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- W2056832018 date "2004-04-30" @default.
- W2056832018 modified "2023-09-26" @default.
- W2056832018 title "Catalysis and Binding of Cyclophilin A with Different HIV-1 Capsid Constructs" @default.
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- W2056832018 doi "https://doi.org/10.1021/bi049841z" @default.
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