Figure 1.
Figure 1 Overall structure of the radixin FERM domain bound to
the ICAM-2 tail peptide. (A) Views of the radixin FERM domain
bound to the ICAM-2 peptide by ribbon representations. The
ICAM-2 peptide is shown in blue. The radixin FERM domain
consists of subdomains A (light blue), B (red) and C (brown).
The linkers A -B (residues 83 -95) and B -C (residues 196 -203)
are colored in gray and the C-terminal linker in green. (B) The
ICAM-2 peptide model in a 2F[o]-F[c] electron density map
countered at the 1 level.
The amino acid residues are indicated with labels of one-letter
codes. Labels in parentheses indicate the terminal residues
whose side chains were not defined in the map. (C) The
28-residue peptide synthesized based on the sequence of the
mouse ICAM-2 cytoplasmic tail was used for the structural work.
Basic residues are in blue. This peptide has two basic regions
and a non-polar region between them. The 16 residues of the
peptide defined on the current map are boxed. Key residues in
binding to the radixin FERM domain are underlined (see text).
The short -strand
(residues 7 -10) and one 3[10] helix (resides 12 -15) are
indicated with an arrow and a cylinder.
level.
The amino acid residues are indicated with labels of one-letter
codes. Labels in parentheses indicate the terminal residues
whose side chains were not defined in the map. (C) The
28-residue peptide synthesized based on the sequence of the
mouse ICAM-2 cytoplasmic tail was used for the structural work.
Basic residues are in blue. This peptide has two basic regions
and a non-polar region between them. The 16 residues of the
peptide defined on the current map are boxed. Key residues in
binding to the radixin FERM domain are underlined (see text).
The short 
-strand
(residues 7 -10) and one 3[10] helix (resides 12 -15) are
indicated with an arrow and a cylinder.