<p>A. Cartoon representation of NRLLLTG-bound HSP70 SBD Molecule A. The SBD and NRLLLTG peptide are shown in magenta and blue, respectively, and all domains and secondary structural elements are labeled. B. Superposition of molecules A and B in the asymmetric unit cell. Molecules A and B are color-coded magenta and green, respectively. C and D. Hinge region between the α and β subdomains. Molecules A and B are shown in panels C and D, respectively. Interacting (MolA) or potential interacting (MolB) residues are indicated in stick and CPK coloring (oxygen in red and nitrogen in blue). The electron density maps corresponding to these residues are contoured at 1.5 (MolA) and 1.0 (MolB) sigma. Hydrogen bonds are indicated with dotted lines.</p
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
<p>The structural variability at each residue position for bound nonameric peptides in p-HLA complex...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
<p>A. Comparison of the NRLLLTG-bound HSP70 SBD to the NRLLLTG-bound DnaK SBD (PDB code 1DKZ). HSP70...
<p>(PDB entry code 4IO8). <b>A</b>, Zoom into the nucleotide binding pocket with NBD in cartoon and ...
<p>A. Omit electron density of the peptide substrate bound to the β subdomain of molecule A is conto...
<p>(A) Superposition of the CTD of SmyD2–SFG (red) and the TPR2 domain of Hop (sky blue) (PDB code 1...
<p>(A) Light grey cartoon represents Hsc70's NBD (PDB: 1BUP) in the “closed” conformation and the gr...
The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve p...
<p>(A) Interactions with HSP90β EDASRMEEVD peptide and (B), with TOMM20 AQSLAEDDVE peptide bound to ...
<p>An overview of three hydrophobic pockets within the SBD domain have been circled and marked as A,...
<p>(A), PyMol cartoon of the HSP90β EDASRMEEVD-peptide (green) bound to the TPR domain of AIP (cyan)...
<p>Crystal structures and domain organization of the additional simulated Hsp70 structures are annot...
The ability of members of the hsp70 family to bind to peptides in vivo and in vitro suggests that th...
The stress-induced 70 kDa heat shock protein (Hsp70) functions as a molecular chaperone to maintain ...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
<p>The structural variability at each residue position for bound nonameric peptides in p-HLA complex...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...
<p>A. Comparison of the NRLLLTG-bound HSP70 SBD to the NRLLLTG-bound DnaK SBD (PDB code 1DKZ). HSP70...
<p>(PDB entry code 4IO8). <b>A</b>, Zoom into the nucleotide binding pocket with NBD in cartoon and ...
<p>A. Omit electron density of the peptide substrate bound to the β subdomain of molecule A is conto...
<p>(A) Superposition of the CTD of SmyD2–SFG (red) and the TPR2 domain of Hop (sky blue) (PDB code 1...
<p>(A) Light grey cartoon represents Hsc70's NBD (PDB: 1BUP) in the “closed” conformation and the gr...
The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve p...
<p>(A) Interactions with HSP90β EDASRMEEVD peptide and (B), with TOMM20 AQSLAEDDVE peptide bound to ...
<p>An overview of three hydrophobic pockets within the SBD domain have been circled and marked as A,...
<p>(A), PyMol cartoon of the HSP90β EDASRMEEVD-peptide (green) bound to the TPR domain of AIP (cyan)...
<p>Crystal structures and domain organization of the additional simulated Hsp70 structures are annot...
The ability of members of the hsp70 family to bind to peptides in vivo and in vitro suggests that th...
The stress-induced 70 kDa heat shock protein (Hsp70) functions as a molecular chaperone to maintain ...
<p><b>Copyright information:</b></p><p>Taken from "The crystal structure of the putative peptide-bin...
<p>The structural variability at each residue position for bound nonameric peptides in p-HLA complex...
<p>(A), (B) and (C): superposition of LCMV (pink) with PV (blue) structures, with the peptide in sti...