Literature summary for 3.4.23.B4 extracted from

Lin, Y.C.; Perryman, A.L.; Olson, A.J.; Torbett, B.E.; Elder, J.H.; Stout, C.D.
Structural basis for drug and substrate specificity exhibited by FIV encoding a chimeric FIV/HIV protease (2011), Acta Crystallogr. Sect. D, 67, 540-548.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant I37V/N55M/V59I/I98S/Q99V/P100N in complex with HIV inhibitors darunavir and lopinavir, to 1.7 and 1.8 A resolution, respectively. A flexible 90s loop and residue 98 play roles in supporting Gag processing and infectivity, residue 37 is involved in the active site and residues 55, 57 and 59 in the flap in conferring the ability to specifically recognize HIV PR drugs. Ile37Val preserves tertiary structure but prevents steric clashes with the inhibitors. Asn55Met and Val59Ile induce a distinct kink in the flap and a new hydrogen bond to darunavir. Ile98Pro-Ser and Pro100Asn increase 90s loop flexibility, Gln99Val contributes hydrophobic contacts to the inhibitors, and Pro100Asn forms compensatory hydrogen bonds	feline immunodeficiency virus

Crystallization (Comment)

Organism

mutant I37V/N55M/V59I/I98S/Q99V/P100N in complex with HIV inhibitors darunavir and lopinavir, to 1.7 and 1.8 A resolution, respectively. A flexible 90s loop and residue 98 play roles in supporting Gag processing and infectivity, residue 37 is involved in the active site and residues 55, 57 and 59 in the flap in conferring the ability to specifically recognize HIV PR drugs. Ile37Val preserves tertiary structure but prevents steric clashes with the inhibitors. Asn55Met and Val59Ile induce a distinct kink in the flap and a new hydrogen bond to darunavir. Ile98Pro-Ser and Pro100Asn increase 90s loop flexibility, Gln99Val contributes hydrophobic contacts to the inhibitors, and Pro100Asn forms compensatory hydrogen bonds

feline immunodeficiency virus

Protein Variants

Protein Variants	Comment	Organism
I37V/N55M/V59I/I98S/Q99V/P100N	chimeric feline immunodeficiency virus protease that supports infectivity but confers sensitivity to the human immunodeficiency virus protease inhibitors darunavir and lopinavir. The protease has five replacements mimicking homologous residues in HIV protease and a sixth which mutated from Pro to Ser during selection	feline immunodeficiency virus

Organism

Organism	UniProt	Comment	Textmining
feline immunodeficiency virus	P16088	Pol polyprotein including protease	-

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Release 2023.1 (January 2023)