How Cyclophilin A Works
Author Information
Author(s): Leone Vanessa, Lattanzi Gianluca, Molteni Carla, Carloni Paolo
Primary Institution: International School for Advanced Studies (SISSA), Trieste, Italy
Hypothesis
The study investigates the mechanism of action of cyclophilin A in catalyzing prolyl isomerization in the HIV-1 capsid protein.
Conclusion
The enzyme cyclophilin A stabilizes a specific cis conformer of the HIV-1 capsid protein, facilitating its isomerization.
Supporting Evidence
- Cyclophilin A significantly stabilizes the cis conformation of the HIV-1 capsid protein.
- The study provides a novel four-step mechanism for the enzymatic process.
- The findings are consistent with available molecular biology data.
Takeaway
Cyclophilin A helps a protein change shape, which is important for how the virus works. Understanding this can help in making new medicines.
Methodology
The study used metadynamics simulations to explore the isomerization of a peptide in water and in complex with cyclophilin A.
Limitations
The accuracy of the force field used in simulations may affect the results, particularly for transition states.
Digital Object Identifier (DOI)
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