From: HIV-1 Tat amino acid residues that influence Tat-TAR binding affinity: a scoping review
Tat amino acid region | Mutation | Binding affinity (Kd) | Percentage increase/decrease in binding affinity | Technique | References |
---|---|---|---|---|---|
30–46 | C34S, C37W | 7.16 × 10−8 M | 19.7% decrease | Nuclear Magnetic Resonance Spectroscopy (NMR) and Fluorescence spectroscopy | [70] |
47–58 | R49A, Q54A | 1.7 × 10−7 M | 142% decrease | Fluorescence resonance energy transfer (FRET), MALDI-TOFMS and Fluorescence binding assay | [82] |
R52A, R53A |  > 100 X 10−9 M |  > 1566% decrease | Electrophoretic mobility shift assay (EMSA) | [69] | |
R55A, R56A |  > 100 X 10−9 M |  > 1566% decrease | EMSA | [69] | |
R55K, R56K | 4 × 10−9 M | 33% increase | EMSA | [69] | |
R52K, R53K | 13 X 10−9 M | 116% decrease | EMSA | [69] | |
R52A, R55A |  > 100 X 10−9 M |  > 1566% decrease | EMSA | [69] | |
R52A, R56A |  > 100 X 10−9 M |  > 1566% decrease | EMSA | [69] | |
R53A, R55A |  > 100 X 10−9 M |  > 1566% decrease | EMSA | [69] | |
R53A, R56A |  > 100 X 10−9 M |  > 1566% decrease | EMSA | [69] | |
K50A, K51A, Q54A | 2.9 × 10−6 M | 4042% decrease | FRET, MALDI-TOFMS and Fluorescence binding assay | [82] | |
R49K, R55K, R56K, R57K | 5 × 10−10 M | 25% decrease | Gel electrophoresis and circular dichroism (CD) | [83] | |
R49A, K50A, K51A, Q54A | 1.8 × 10−5 M | 21,328.6% decrease | FRET, MALDI-TOFMS and Fluorescence binding assay | [82] | |
R49K, R53K, R55K, R56K, R57K | 9 × 10−10 M | 125% decrease | Gel electrophoresis and CD | [83] | |
R49K, Q54K, R55K, R56K, R57K | 1.8 × 10−9 M | 350% decrease | Gel electrophoresis and CD | [83] | |
R49K, R52K, R53K, R56K, R57K |  > 5 × 10−8 M |  > 12,400% decrease | Gel electrophoresis and CD | [83] | |
R49K, R52K, R53K, R55K, R57K |  > 1 × 10−7 M |  > 24,900% decrease | Gel electrophoresis and CD | [83] | |
R49K, R53K, Q54K, R55K, R56K, R57K | 7 × 10−10 M | 75% decrease | Gel electrophoresis and CD | [83] | |
R49K, R52K, R54K, R55K, R56K, R57K | 3.5 × 10−9 M | 775% decrease | Gel electrophoresis and CD | [83] | |
R49K, R52K, R53K, R55K, R56K, R57K | 3.2 × 10–8 | 1428% decrease | EMSA and Anisotropy assay | [84] | |
R49A, K50A, Q54A, K51R, R53A, Q54R, R57A | 6.6 × 10−5 M | 94,185% decreased | FRET, MALDI-TOFMS and Fluorescence binding assay | [82] | |
R49A, K50A, R51R, R53A, Q54R, R56A, R57A | No binding | No binding | FRET, MALDI-TOFMS and Fluorescence binding assay | [82] | |
R49A, K50A, K51R, R53A, Q54R, R55A, R56A, R57A | No binding | No binding | FRET, MALDI-TOFMS and Fluorescence binding assay | [82] | |
G48K, R49K, R52K, R53K, Q54K, R55K, R56K, R57A | 1.5 × 10–6 M | 275% decrease | Electron paramagnetic resonance spectroscopy (EPR) | [72] |