Figure 3.
Figure 3: Detailed interaction between TRAF2 and the TNF-R2
peptide. a,Simulated annealing omit difference map for the
TNF-R2 peptide calculated with reflections between 20.0 and 2.3
Å resolution and contoured at 2.0 .
The peptide model is superimposed. b, Molecular surface of a
TRAF2 promoter, showing the bound TNF-R2 peptide as a stick
model; the three-fold axis is in the vertical orientation.
Surface colour coding is according to electrostatic surface
potential, scaled from -30 to +30 kTe^-1, with blue for positive
and red for negative. Selected residues in the receptor peptide
and the underlying secondary-structural elements of TRAF2 at the
binding site are labelled. c, Stereo view of the detailed
interaction between the TNF-R2 peptide (carbon atoms shown in
yellow) and the TRAF2 protomer (carbon atoms shown in grey). The
main chain of the TRAF2 structure is shown in cyan as backbone
worms. Selected residues in the peptide (primed numbers in
green) and the protein (in grey) are labelled. Hydrogen bonds
and a salt bridge are shown as black dotted lines.
.
The peptide model is superimposed. b, Molecular surface of a
TRAF2 promoter, showing the bound TNF-R2 peptide as a stick
model; the three-fold axis is in the vertical orientation.
Surface colour coding is according to electrostatic surface
potential, scaled from -30 to +30 kTe^-1, with blue for positive
and red for negative. Selected residues in the receptor peptide
and the underlying secondary-structural elements of TRAF2 at the
binding site are labelled. c, Stereo view of the detailed
interaction between the TNF-R2 peptide (carbon atoms shown in
yellow) and the TRAF2 protomer (carbon atoms shown in grey). The
main chain of the TRAF2 structure is shown in cyan as backbone
worms. Selected residues in the peptide (primed numbers in
green) and the protein (in grey) are labelled. Hydrogen bonds
and a salt bridge are shown as black dotted lines.