Fig. 3: Structure of PRPF40A tandem WW domains in complex with SF1WWbs peptide. | Nature Communications

Fig. 3: Structure of PRPF40A tandem WW domains in complex with SF1WWbs peptide.

From: Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs

Fig. 3

A Cartoon representation of WW12 tandem of PRPF40A bound to the SF1WWbs peptide (PPLPPGAPPPPPPPPP, shown in sticks), indicating the recognition of the three segments in the peptide and the aromatic residues involved in the interaction. B Cartoon and surface view of the WW domains of PRPF40A, in the same orientation (WW1 left, WW2 right), with the interacting SF1 peptide depicted in sticks. The amino acids recognized by the canonical interface are labeled. C Zoom view of the stick representation of Trp 168 (WW1) sandwiched by the PPGAP motif of SF1: this Pro-Trp-Pro stacking interaction has not been observed in other WW domain interactions with proline-rich peptides.

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