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Figure 2.
Crystal structure of the FERM-CD44 complex. A, ribbon
representations of the radixin FERM domain complexed with the
CD44 cytoplasmic peptide (blue). The radixin FERM domain
comprises three subdomains: A (residues 3-82 in green), B
(residues 96-195 in red), and C (residues 204-297 in yellow).
Linkers A-B (residues 83-95) and B-C (residues 196-203) are
colored gray. B, surface electrostatic potentials of the FERM
domain and a close-up view of the CD44 cytoplasmic peptide
docked into the groove formed between helix α1C and strand β5C
of subdomain C. The peptide is shown as a stick model (labeled
with one-letter codes), and the four side chain-binding sites
(S1--S4) for the bound β strand of CD44 and the deep
hydrophobic pocket (P1) are labeled and indicated with yellow
dashed circles. Site S4 adjoins pocket P1. C, a stick model of
the CD44 cytoplasmic peptide is shown in the omit electron
density map for the CD44 cytoplasmic peptide at the contour
level of 1σ.
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