Figure 6.
Fig. 6. Ribbon drawing of the NMR reference structure of
the complex between Pin1 WW domain (in light blue) and
phosphopeptide ligand (in red), in comparison with the
orientation of the CTD peptide (in violet) from the
crystallographic model of the complex (13). The image was
obtained by backbone superimposition of WW domains from our NMR
complex and from the CTD peptide/Pin1 complex (13). Only the WW
domain from this study and both phosphopeptide ligands are
represented. Side chains implicated into the binding interface
are labeled (in white for the WW domain residues and yellow for
the ligand residues) and depicted in detail, as well as the
amino acid pair Trp6-Pro32 of the WW domain. N atoms are blue
and P atoms are violet. C atoms are green in the WW domain and
orange in the tau ligand.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
25150-25156)
copyright 2001.
phosphopeptide ligand (in red), in comparison with the
orientation of the CTD peptide (in violet) from the
crystallographic model of the complex (13). The image was
obtained by backbone superimposition of WW domains from our NMR
complex and from the CTD peptide/Pin1 complex (13). Only the WW
domain from this study and both phosphopeptide ligands are
represented. Side chains implicated into the binding interface
are labeled (in white for the WW domain residues and yellow for
the ligand residues) and depicted in detail, as well as the
amino acid pair Trp6-Pro32 of the WW domain. N atoms are blue
and P atoms are violet. C atoms are green in the WW domain and
orange in the tau ligand.