Literature summary for 3.4.23.16 extracted from

Swairjo, M.A.; Towler, E.M.; Debouck, C.; Abdel-Meguid, S.S.
Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus Protease (1998), Biochemistry, 37, 10928-10936.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
determination of the crystal structures of three chimeric HIV proteases complexed with SB203386. The chimeras are constructed by substituting amino acid residues in the HIV type 1 protease sequence with the corresponding residues from HIV type 2 in the region spanning residues 31-37 and in the active site cavity. 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 affinity and mode of binding (two inhibitor molecules per protease dimer). However, further substitution of active site residues 47 and 82 has a compensatory effect which restores the HIV-1-like inhibitor binding mode	Human immunodeficiency virus 1

Crystallization (Comment)

Organism

determination of the crystal structures of three chimeric HIV proteases complexed with SB203386. The chimeras are constructed by substituting amino acid residues in the HIV type 1 protease sequence with the corresponding residues from HIV type 2 in the region spanning residues 31-37 and in the active site cavity. 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 affinity and mode of binding (two inhibitor molecules per protease dimer). However, further substitution of active site residues 47 and 82 has a compensatory effect which restores the HIV-1-like inhibitor binding mode

Human immunodeficiency virus 1

Protein Variants

Protein Variants	Comment	Organism
additional information	three chimeric HIV proteases are constructed by substituting amino acid residues in the HIV type 1 protease sequence with the corresponding residues from HIV type 2 in the region spanning residues 31-37 and in the active site cavity. 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 affinity and mode of binding (two inhibitor molecules per protease dimer). However, further substitution of active site residues 47 and 82 has a compensatory effect which restores the HIV-1-like inhibitor binding mode	Human immunodeficiency virus 1

Inhibitors

Inhibitors	Comment	Organism	Structure
SB203386	-	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000018	-	SB203386	-	Human immunodeficiency virus 1