2BPX

HIV-1 protease-inhibitor complex

Summary for 2BPX

• Entry DOI: 10.2210/pdb2bpx/pdb
• Descriptor: HIV-1 PROTEASE, N-[2(R)-HYDROXY-1(S)-INDANYL]-5-[(2(S)-TERTIARY BUTYLAMINOCARBONYL)-4(3-PYRIDYLMETHYL)PIPERAZINO]-4(S)-HYDROXY-2(R)-PHENYLMETHYLPENTANAMIDE (3 entities in total)
• Functional Keywords: acid protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P04587
• Total number of polymer chains: 2
• Total formula weight: 22221.30

Authors

Munshi, S.,Chen, Z. (deposition date: 1998-01-22, release date: 1999-02-23, Last modification date: 2024-02-14)

Primary citation

Munshi, S.,Chen, Z.,Li, Y.,Olsen, D.B.,Fraley, M.E.,Hungate, R.W.,Kuo, L.C.
Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.
Acta Crystallogr.,Sect.D, 54:1053-1060, 1998

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.

PubMed: 9757136
DOI: 10.1107/S0907444998003588

Experimental method

X-RAY DIFFRACTION (2.8 Å)