2BB9

Structure of HIV1 protease and AKC4p_133a complex.

Summary for 2BB9

• Entry DOI: 10.2210/pdb2bb9/pdb
• Descriptor: Protease, 2-ETHOXYETHYL (1S,2S)-3-{(2S)-4-[(3AS,8S,8AR)-2-OXO-3,3A,8,8A-TETRAHYDRO-2H-INDENO[1,2-D][1,3]OXAZOL-8-YL]-2-BENZYL-3-OXO-2,3-DIHYDRO-1H-PYRROL-2-YL}-1-BENZYL-2-HYDROXYPROPYLCARBAMATE (3 entities in total)
• Functional Keywords: protease, hydrolase
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 22233.22

Authors

Smith III, A.B.,Charnley, A.K.,Kuo, L.C.,Munshi, S. (deposition date: 2005-10-17, release date: 2005-11-15, Last modification date: 2023-08-23)

Primary citation

Smith III, A.B.,Charnley, A.K.,Harada, H.,Beiger, J.J.,Cantin, L.D.,Kenesky, C.S.,Hirschmann, R.,Munshi, S.,Olsen, D.B.,Stahlhut, M.W.,Schleif, W.A.,Kuo, L.C.
Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors possessing augmented P2' side chains
Bioorg.Med.Chem.Lett., 16:859-863, 2006

PubMed Abstract: A series of monopyrrolinone-based HIV-1 protease inhibitors possessing rationally designed P2' side chains have been synthesized and evaluated for activity against wild-type HIV-1 protease. The most potent inhibitor displays subnanomolar potency in vitro for the wild-type HIV-1 protease. Additionally, the monopyrrolinone inhibitors retain potency in cellular assays against clinically significant mutant forms of the virus. X-ray structures of these inhibitors bound in the wild-type enzyme reveal important insights into the observed biological activity.

PubMed: 16298527
DOI: 10.1016/j.bmcl.2005.11.011

Experimental method

X-RAY DIFFRACTION (1.35 Å)