Download MendeleyRapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.
Munshi, S., Chen, Z., Li, Y., Olsen, D.B., Fraley, M.E., Hungate, R.W., Kuo, L.C.(1998) Acta Crystallogr D Biol Crystallogr 54: 1053-1060
- PubMed: 9757136
- DOI: https://doi.org/10.1107/s0907444998003588
- Primary Citation of Related Structures:
2BPV, 2BPW, 2BPX, 2BPY, 2BPZ - PubMed Abstract:
The ability to replace an inhibitor bound to the HIV-1 protease in single crystals with other potent inhibitors offers the possibility of investigating a series of protease inhibitors rapidly and conveniently with the use of X-ray crystallography. This approach affords a fast turnaround of structural information for iterative rational drug designs and obviates the need for studying the complex structures by co-crystallization. The replacement approach has been successfully used with single crystals of the HIV-1 protease complexed with a weak inhibitor. The structures of the complexes obtained by the replacement method are similar to those determined by co-crystallization.
Organizational Affiliation:
Department of Antiviral Research, Merck Research Laboratories, West Point, PA 19486, USA.
