1FQX

CRYSTAL STRUCTURE OF THE COMPLEX OF HIV-1 PROTEASE WITH A PEPTIDOMIMETIC INHIBITOR

Summary for 1FQX

• Entry DOI: 10.2210/pdb1fqx/pdb
• Related PRD ID: PRD_000386
• Descriptor: PROTEASE RETROPEPSIN, N-{(2S,3S)-3-[(tert-butoxycarbonyl)amino]-2-hydroxy-4-phenylbutyl}-L-phenylalanyl-L-alpha-glutamyl-L-phenylalaninamide (3 entities in total)
• Functional Keywords: aspartyl protease, protease, hiv, peptidomimetic, inhibitor, drug design, hydroxyethylamine isostere, 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): P03367
• Total number of polymer chains: 2
• Total formula weight: 22311.34

Authors

Dohnalek, J.,Hasek, J.,Duskova, J.,Petrokova, H.,Hradilek, M.,Soucek, M.,Konvalinka, J.,Brynda, J.,Sedlacek, J.,Fabry, M. (deposition date: 2000-09-07, release date: 2001-03-14, Last modification date: 2024-02-07)

Primary citation

Dohnalek, J.,Hasek, J.,Duskova, J.,Petrokova, H.,Hradilek, M.,Soucek, M.,Konvalinka, J.,Brynda, J.,Sedlacek, J.,Fabry, M.
A distinct binding mode of a hydroxyethylamine isostere inhibitor of HIV-1 protease.
Acta Crystallogr.,Sect.D, 57:472-476, 2001

PubMed Abstract: Crystallization conditions for an HIV-1 protease-inhibitor complex were optimized to produce crystals suitable for X-ray diffraction experiments. The X-ray structure of the HIV-1 protease complex was solved and refined at 3.1 A resolution. In contrast to Saquinavir, the mimetic hydroxy group of the inhibitor Boc-Phe-Psi[(S)-CH(OH)CH(2)NH]-Phe-Glu-Phe-NH(2) is placed asymmetrically with respect to the non-crystallographic twofold axis of the protease dimer so that hydrogen bonds between the amino group of the inhibitor and the catalytic aspartates can be formed. The inhibitor binds in the centre of the active site by a compact network of hydrogen bonds to Gly27, Gly127, Asp25, Asp125 and via the buried water molecule W301 to Ile50 and Ile150.

PubMed: 11223536
DOI: 10.1107/S0907444900018928

Experimental method

X-RAY DIFFRACTION (3.1 Å)