Comparison of the Ssn6 NTpolyQ_TPR1-3 models with known TPR structures/interactions from the literature.

(Left) Cartoon representations of the final models shown in Fig 5 with a slightly different coloring: the N11 is colored in magenta, for comparison. The known 3D-structures from the literature shown in this figure correspond to the following PDB entries: 1IYG (solution structure of a Fis1-like protein from a mouse cDNA, unpublished); 1ELR (crystal structure of the TPR2 domain of human Hop in complex with an Hsp90 peptide [18]); 3ZFW (crystal structure of the TPR-like domain of KLC2 in complex with a cargo peptide [50]); 2PQR (crystal structure of yeast Fis1p in complex with a fragment of yeast Caf4p [22]); 3GZ1 (crystal structure of the IpgC chaperone from Shigella flexneri in complex with the chaperone binding region of IpgBp [24]) and 3KS2 (crystal structure of a truncated IpgC fragment showing an alternative head-to-head dimerization mode of this chaperone [25]). Molecules participating in dimer formation (obtained from symmetry-related molecules in the corresponding crystal structures) are depicted as ribbon models and indicated as accentuated words. Met10 of Ssn6 and important hydrophobic residues of linear ligand peptides in known TPR-mediated complexes are depicted in sticks and are labeled. Arrows indicate helical regions of the known crystal structures that are spatially similar to the Qx16 and N11 helices in model-1.