|
Figure 3.
Figure 3. Structural and Dynamic Features of the Hsp90
Peptide Binding Site
(A) Conserved polar two-carboxylate
clamp residues are shown in purple; additional residues
consistently involved in ligand binding are shown in pale blue.
Residues that are physically distinct between Hop and Ppp5 and
whose variation is responsible for the different binding modes
of the Hsp90 peptide between those complexes are shown in gray.
(B) Extent of side chain assignment shown on the surface of
the TPR domain (rotated 90° with respect to [A]). Unassigned
resonances are shown in red, assigned resonances are shown in
green, and the peptide is shown as a stick model. The absence of
side chain resonances from the spectra suggests that the
affected chemical groups are undergoing significant microsecond
to millisecond timescale motion.
|
