Figure 2.
Figure 2 The ICAM-2 tail peptide recognition by the radixin FERM
domain. (A) Surface electrostatic potentials of the radixin FERM
domain 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 ICAM-2 peptide found
in the complex crystal is shown in a stick model. The disordered
C-terminal basic region is indicated by an arrow of dotted
lines. (B) The ICAM-2 binding groove on subdomain C is formed
primarily by hydrophobic residues from helix 1C
and strand 5C.
The bound ICAM-2 peptide is shown in a transparency ribbon
model. (C) Schematic representation of the interactions between
the ICAM-2 peptide (blue) and subdomain C (brown). Hydrogen
bonds are shown by broken lines. (D) The ICAM-2 peptide found in
the FERM -ICAM-2 complex is shown in a stick model (light blue)
with their interacting residues from subdomain C (brown).
Hydrogen bonds are shown by dotted lines. (E) A close-up view of
the hydrophobic and hydrogen bonding interactions between the
ICAM-2 peptide and the FERM domain mediated by His288 from
subdomain C.
1C
and strand 
5C.
The bound ICAM-2 peptide is shown in a transparency ribbon
model. (C) Schematic representation of the interactions between
the ICAM-2 peptide (blue) and subdomain C (brown). Hydrogen
bonds are shown by broken lines. (D) The ICAM-2 peptide found in
the FERM -ICAM-2 complex is shown in a stick model (light blue)
with their interacting residues from subdomain C (brown).
Hydrogen bonds are shown by dotted lines. (E) A close-up view of
the hydrophobic and hydrogen bonding interactions between the
ICAM-2 peptide and the FERM domain mediated by His288 from
subdomain C.