1bdr | pdb_00001bdr
HIV-1 (2: 31, 33-37) PROTEASE COMPLEXED WITH INHIBITOR SB203386
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Overview
The structural basis of ligand specificity in human immunodeficiency virus, (HIV) protease has been investigated by determining the crystal structures, of three chimeric HIV proteases complexed with SB203386, a tripeptide, analogue inhibitor. The chimeras are constructed by substituting amino, acid residues in the HIV type 1 (HIV-1) protease sequence with the, corresponding residues from HIV type 2 (HIV-2) in the region spanning, residues 31-37 and in the active site cavity. SB203386 is a potent, inhibitor of HIV-1 protease (Ki = 18 nM) but has a decreased affinity for, HIV-2 protease (Ki = 1280 nM). Crystallographic analysis reveals that, substitution of residues 31-37 (30's loop) with those of HIV-2 protease, renders the chimera similar to HIV-2 protease in both the inhibitor, binding ... [(full description)]
About this Structure
1BDR is a [Single protein] structure of sequence from [Human immunodeficiency virus 1] with IM1 as [ligand]. Active as [[1]], with EC number [3.4.23.16]. Full crystallographic information is available from [OCA].
Reference
Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease., Swairjo MA, Towler EM, Debouck C, Abdel-Meguid SS, Biochemistry. 1998 Aug 4;37(31):10928-36. PMID:9692985
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