Structural analyses of 2015-updated drug-resistant mutations in HIV-1 protease: an implication of protease inhibitor cross-resistance

Table 4 Structural characterized features used in the graph constructions for the PI-resistance mutants to TPV

	Vpocket^a (Å³)	AllosComm^b	ΔΔG score / ΔS^c (kcal/mol)	RMSd (Å)
Tipranavir (TPV) — molecular weight = ~603 g/mol
TPV_0 (major/minor)	1912.49 (1963.76)	0.627 (0.277)	3.54 / 0.42	0.97
TPV_1 (major/minor)	1858.07	0.741 (0.795)	8.99 / 3.12	1.03
TPV_2 (major/minor)	1804.05	0.905 (0.287)	0.90 / 0.7	1.05
TPV_3 (minor)	2228.93	0.24 (0.379)	4.43 / 1.3	1.02

^aPocket volume of the native protease [PDB: 1ODW], which contains no mutations in the presence of corresponding PIs, is shown in parentheses for comparison purpose
^bFor comparison purposes of allosteric effect, communication estimated values of the native protease were shown in parentheses
^cΔΔG and ΔS scores represent free energy and vibrational energy respectively, demonstrating thermo-stability of the protease when mutated from the native protease

ISSN: 1471-2105