3WSJ

HTLV-1 protease in complex with the HIV-1 protease inhibitor Indinavir

Summary for 3WSJ

Entry DOI	10.2210/pdb3wsj/pdb
Related	3LIX
Descriptor	Protease, N-[2(R)-HYDROXY-1(S)-INDANYL]-5-[(2(S)-TERTIARY BUTYLAMINOCARBONYL)-4(3-PYRIDYLMETHYL)PIPERAZINO]-4(S)-HYDROXY-2(R)-PHENYLMETHYLPENTANAMIDE, SULFATE ION, ... (5 entities in total)
Functional Keywords	retroviral protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Human T-lymphotropic virus 1
Total number of polymer chains	2
Total formula weight	27189.99
Authors	Kuhnert, M.,Steuber, H.,Diederich, W.E. (deposition date: 2014-03-14, release date: 2014-10-22, Last modification date: 2023-11-08)
Primary citation	Kuhnert, M.,Steuber, H.,Diederich, W.E. Structural basis for HTLV-1 protease inhibition by the HIV-1 protease inhibitor indinavir. J.Med.Chem., 57:6266-6272, 2014 Cited by PubMed Abstract: HTLV-1 protease (HTLV-1 PR) is an aspartic protease which represents a promising drug target for the discovery of novel anti-HTLV-1 drugs. The X-ray structure of HTLV-1 PR in complex with the well-known and approved HIV-1 PR inhibitor Indinavir was determined at 2.40 Å resolution. In this contribution, we describe the first crystal structure in complex with a nonpeptidic inhibitor that accounts for rationalizing the rather moderate affinity of Indinavir against HTLV-1 PR and provides the basis for further structure-guided optimization strategies. PubMed: 25006983 DOI: 10.1021/jm500402c PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.404 Å)

Structure validation