Fig. 6: Binding selectivity of WW-containing proteins and potential roles of PRPF40A during splicing. | Nature Communications

Fig. 6: Binding selectivity of WW-containing proteins and potential roles of PRPF40A during splicing.

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

Fig. 6

A Selectivity mechanisms of WW-containing proteins. The different layers of WW domain specificity towards the recognition of Pro-rich peptides start with the intrinsic preference for certain motifs. The selectivity gets increased with these domains combined in tandems and it is even higher if the domains show interdomain contacts upon binding to the right sequences. Finally, the additional layer of selectivity comes from the role of the regulatory regions nearby the WW domains that are able to compete out those suboptimal binding events. B Diagram showing the percentage of all human proteins containing a tandem of WW domains that also have proline-rich sequences and examples of some of those proteins as schematic domain representations (C). D Potential roles of PRPF40A in early spliceosome assemblies. PRPF40A role in bridging the branch point region of the intron and the 5′splicing site could be important for (1) the intron definition events, when the exon definition cannot happen, like in the microexon regulation (left), (2) reinforcement of the A complex bridging (middle) and/or (3) in those events that happen co-transcriptionally due to its shown interaction with the C-terminal domain of the RNA polymerase II (right).

Back to article page