|
Figure 2.
Figure 2. The FERM-NHERF Interactions
(A) Front (left)
and side (right) views of surface electrostatic potentials of
the radixin FERM domain. The front view is viewed from the same
direction as in Figure 1A. Positive (blue, +14 kT/e) and
negative (red, −14 kT/e) potentials are mapped on the van der
Waals surfaces. The four crystallographic-independent NHERF-1
peptides are shown in tube models (cyan). A side view of the
FERM domain is shown without the NHERF-1 peptide to show two
hydrophobic pockets for the Trp348 and Phe355 side chains from
the NHERF peptide.
(B) A close-up view of the amphipathic
helix of the NHERF-1 peptide (cyan) docked to the groove formed
by the β sandwich of subdomain C (yellow). Hydrogen bonds are
shown with dotted lines. The C-terminal carboxyl group of Leu358
is labeled with CPX.
(C) Schematic diagram of the
interaction between the NHERF-1 peptide (residues 339–358,
cyan main chain bonds) and the FERM domain (brown main chain
bonds) with atom colors: black, C; blue, N; red, O; yellow, S.
Polar contacts are shown with red, dashed lines, and hydrophobic
contacts are indicated by arcs with radiating spokes. A list of
all residues involved in binding either peptide together with
their distances is given in Table S2.
(D) A close-up
view of the superimposed C-terminal region of NHERF-1 (blue)
and NHERF-2 (yellow) peptides bound to the FERM domains. Leu354
and the C-terminal end residue of NHERF-1, Leu358, are replaced
with Ile333 and Phe337 in NHERF-2, respectively. These residues
interact with residues from the FERM domains drawn in cyan
(NHERF-1 bound form) and gray (NHERF-2 bound form).
|
