<p>(a) Native-DNA complex, (b) R273C-DNA complex, (c) R273H-DNA complex, (d) R273C_T284R-DNA complex, (e) R273H_T284R-DNA complex and (f) R273H_S240R-DNA complex. The color coding represents the p53 protein in brown color, DNA in purple color. Hydrogen bonding interactions are denoted by dashed lines. This figure was prepared by Ligplot.</p
<p>(<b>A</b>) Intermolecular hydrogen bonds between Ets1 and the neighboring DNA duplex within (Ets1...
<p><b>A.</b> X-ray model showing all the residues at the interface. The color scheme is the same as ...
(A) Samplings of p53’s C-terminal linker (yellow) and iASPP’s RT loop (red) from 3 ×1 μs all-atom MD...
<p>A, The loop-sheet-helix interaction interface between two p53 molecules revealed by the crystal s...
<p>Color scheme: native (black), R131W (red), R131Q (green), and R203C (blue).The R203C mutant compl...
<p>Dehydrons in the protein are depicted by green bars joining the two residues paired by the HB, wh...
<p>(a) Native, R273C and R273C_T284R, (b) Native, R273H and R273H_T284R, (c) Native, R273H and R273H...
<div><p>(A) The primary sequence of p53 comprising 393 amino acid residues was retrieved from Unipro...
(A) The protein’s molecular surface is shown in grey. Loop L1, where compound 2 is covalently bound,...
<div><p>(A) Three close-up views of the protein–DNA interaction observed in the T-ag obd–DNA co-stru...
<p>Reactive phosphate group in DNA is marked with a red asterisk. (a) Tm1631-DNA model, residues tha...
<p>Histograms report the number of Arg and Lys interatomic contacts in DNA (A, B) and RNA (C, D) int...
The protein (brown) and DNA (light blue) are shown in cartoon representation. The QGR motif and R93 ...
<p>(A) Schematic view of the domain structure of p53. The 393-residue p53 protein comprises an N-ter...
<div><p>(A) Schematic representation of σ<sub>4</sub>–DNA interactions for <i>Ec</i> σ<sup>E</sup><s...
<p>(<b>A</b>) Intermolecular hydrogen bonds between Ets1 and the neighboring DNA duplex within (Ets1...
<p><b>A.</b> X-ray model showing all the residues at the interface. The color scheme is the same as ...
(A) Samplings of p53’s C-terminal linker (yellow) and iASPP’s RT loop (red) from 3 ×1 μs all-atom MD...
<p>A, The loop-sheet-helix interaction interface between two p53 molecules revealed by the crystal s...
<p>Color scheme: native (black), R131W (red), R131Q (green), and R203C (blue).The R203C mutant compl...
<p>Dehydrons in the protein are depicted by green bars joining the two residues paired by the HB, wh...
<p>(a) Native, R273C and R273C_T284R, (b) Native, R273H and R273H_T284R, (c) Native, R273H and R273H...
<div><p>(A) The primary sequence of p53 comprising 393 amino acid residues was retrieved from Unipro...
(A) The protein’s molecular surface is shown in grey. Loop L1, where compound 2 is covalently bound,...
<div><p>(A) Three close-up views of the protein–DNA interaction observed in the T-ag obd–DNA co-stru...
<p>Reactive phosphate group in DNA is marked with a red asterisk. (a) Tm1631-DNA model, residues tha...
<p>Histograms report the number of Arg and Lys interatomic contacts in DNA (A, B) and RNA (C, D) int...
The protein (brown) and DNA (light blue) are shown in cartoon representation. The QGR motif and R93 ...
<p>(A) Schematic view of the domain structure of p53. The 393-residue p53 protein comprises an N-ter...
<div><p>(A) Schematic representation of σ<sub>4</sub>–DNA interactions for <i>Ec</i> σ<sup>E</sup><s...
<p>(<b>A</b>) Intermolecular hydrogen bonds between Ets1 and the neighboring DNA duplex within (Ets1...
<p><b>A.</b> X-ray model showing all the residues at the interface. The color scheme is the same as ...
(A) Samplings of p53’s C-terminal linker (yellow) and iASPP’s RT loop (red) from 3 ×1 μs all-atom MD...