Figure 3.
Figure 3. Residues of the EH domain interacting with NPF[Hrb(L
arrow
R)]. a, Binding site interactions. EH[2] is represented as a
partially transparent surface with the protein backbone from
residue 145 -175 displayed as a blue ribbon. Black arrows at the
top of the figure indicate the direction of the backbone.
Residues of EH[2] are depicted in ball-and-stick representation
with C, N, O, and calcium atoms in blue, dark blue, red, and
green, respectively. The peptide residues NPFR are displayed as
stick models with C, N, and O atoms colored orange, blue and
red, respectively. Phe, Arg and Asn side chain protons are shown
in white. Potential hydrogen bonds involving NPF[Hrb(L arrow
R)] are indicated by green lines. The carbonyl atoms of Leu 165
and Gly 166 are part of helix C,
and putative hydrogen bonds with the HN protons (in white) of
Trp 169 and Glu 170 are indicated by yellow lines. b, View of
the binding site rotated 180°
about a vertical axis to highlight the interactions with the Pro
and Phe residues of NPF, using the same color scheme as in (a).
c, Degree of amino acid conservation of EH residues that contact
the TNPFR sequence. EH[ 2] is shown as a color coded surface
with different shades of blue representing the degree of
conservation as defined in the insert. The labeling stands for a
single, pair or triplet of amino acids that are conserved at
that position. The first letter and the number indicate the
residue and sequence number of EH[2], respectively. NPF residues
are shown in orange, T and R are displayed in yellow. Figs 1,
3a, b were generated using InsightII (Biosym Inc.), and Fig. 3c
using VMD^30.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2000,
7,
1018-1022)
copyright 2000.
arrow
R)]. a, Binding site interactions. EH[2] is represented as a
partially transparent surface with the protein backbone from
residue 145 -175 displayed as a blue ribbon. Black arrows at the
top of the figure indicate the direction of the backbone.
Residues of EH[2] are depicted in ball-and-stick representation
with C, N, O, and calcium atoms in blue, dark blue, red, and
green, respectively. The peptide residues NPFR are displayed as
stick models with C, N, and O atoms colored orange, blue and
red, respectively. Phe, Arg and Asn side chain protons are shown
in white. Potential hydrogen bonds involving NPF[Hrb(L 
C,
and putative hydrogen bonds with the HN protons (in white) of
Trp 169 and Glu 170 are indicated by yellow lines. b, View of
the binding site rotated 
180°
about a vertical axis to highlight the interactions with the Pro
and Phe residues of NPF, using the same color scheme as in (a).
c, Degree of amino acid conservation of EH residues that contact
the TNPFR sequence. EH[ 2] is shown as a color coded surface
with different shades of blue representing the degree of
conservation as defined in the insert. The labeling stands for a
single, pair or triplet of amino acids that are conserved at
that position. The first letter and the number indicate the
residue and sequence number of EH[2], respectively. NPF residues
are shown in orange, T and R are displayed in yellow. Figs 1,
3a, b were generated using InsightII (Biosym Inc.), and Fig. 3c
using VMD^30.