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Figure 1.
FIGURE 1. Overall structure of the CMSA·Cbl-b and
CMSA·CD2 heterotrimeric complexes and protein/peptide
interaction details. A and C, CMSA[SH3I] binds the peptides in a
class I orientation (shown in purple), and CMSA[SH3II]
recognizes the peptide in class II orientation (shown in gray).
The Cbl-b peptide is shown in light blue (A) and CD2 peptide in
yellow (B). The  A-weighted electron
density map around them is contoured at 1.0 . Elements of secondary
structure and the positions of the RT, n-Src, and distal loops
are indicated. B and D, Schematic representation of contacts
between CMSA and the Cbl-b (B) and CD2 (D) peptides (light blue
and yellow, respectively). Residues 902, 903, and 904 from the
Cbl-b peptide were not visible at the electron density map.
Residues 324, 325, and 326 from the CD2 peptide are also
disordered. Interactions and residues from SH3I are shown in
purple and in gray for SH3II. Dashed lines show hydrogen bonds
(labeled with peptide-protein distances in Å), and purple
and gray rays designate hydrophobic interactions.
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