Chemistry Reference
In-Depth Information
Fig. 9.10
The leucine zipper
structural motif for the dimer
of general control protein
GCN4 from
Saccharomyces
Cerevisiae
(PDB code entry
1ZIK). The monomer A is
presented in
blue
and the
monomer B in
magenta
.
Leucine residues belonging to
both monomers are presented
in
red
Fig. 9.11
SH2 structural
motif for the human
cytoplasmic protein NCK2
(
blue
ribbon) in complex with
a decaphosphopeptide
(
magenta
, atoms ball and
sticks), PDB code entry 1CIA
A structural motif found in numerous proteins is the tetratricopeptide repeat (TPR)
that facilitates specific interactions with a partner protein (Blatch and Lassle
1999
).
Three-dimensional structural data revealed that a TPR motif contains antiparallel
alpha-helices with an amphipathic channel that might accommodate the complemen-
tary region of a target protein, as it is shown in Fig.
9.13
for human dual specificity
protein kinase MPS1 dimer, PDB code entry 4H7X (Thebault et al.
2012
).
The WW motif is one of the smallest protein domains, composed of 40 amino
acids, which mediates specific protein-protein interactions with short proline-rich or
proline-containing motifs (Chen and Sudol
1995
). The name of this motif comes from
the two tryptophan residues spaced 20-23 amino acids apart and it binds to proteins
with particular proline-motifs and/or phosphoserine-phos-phothreonine-containing
motifs.
