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Figure 3.
Fig. 3. Structural basis of peptoid recognition. (A)
Structure of wild-type Sos peptide (PPPVPPRRR) bound to Crk SH3
domain (20). Proline-rich core binding grooves are indicated by
dashed boxes. Highly conserved surface residues among the four
SH3 domains studied here (one or two conservative amino acid
types) are green. Variable surface residues (3+ amino acid
types) are brown. The ligand PXXP core binds at the most
conserved surface on the protein. (B) Structure of peptide 34
bound to Crk SH3 domain. N-(S)-1-Phenylethyl peptoid side chain
(orange) bound at site P[2]. Close-up view from the same
perspective as above. (C) Structure of peptide 39 bound to the
Sem5 SH3 domain. N-Cyclopropylmethyl peptoid side chain (orange)
bound at site P[  1].
Close-up view from the same perspective as above.
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