1bdr
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(New page: 200px<br /> <applet load="1bdr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bdr, resolution 2.8Å" /> '''HIV-1 (2: 31, 33-37)...)
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Revision as of 15:55, 29 October 2007
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HIV-1 (2: 31, 33-37) PROTEASE COMPLEXED WITH INHIBITOR SB203386
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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