Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.

Abstract

WW domain is a well known protein module that mediates protein to protein interactions by binding to proline-containing ligands. Based on the ligand predilections, the WW domains have been classified into four major groups. Group II and III WW domains have been reported to bind the proline-leucine and proline-arginine motifs, respectively. In the present study, using surface plasmon resonance technique we have shown that these WW domains have almost indistinguishable ligand preferences and kinetic properties. Hence, we propose that Group II and III WW domains should be joined together as one group (Group II/III). Unlike Group I and IV WW domains, Group II/III WW domains can bind simple polyprolines as well as the proline-leucine and proline-arginine motifs, and they possess two Xaa-proline (where Xaa is any amino acid) binding grooves similar to SH3 domains. Our work assigns Group II and III WW domains to a larger family of polyproline-binding modules and proteins, which includes SH3 domains and profilin. Because polyprolines belong to the most frequently found peptide motifs in several genomes, our study implies the versatile importance of Group II/III WW domains in signaling.

Statistics

0204060'05'06'07'08'09'10'11'12'13'14'15'16'17
Citations per Year

122 Citations

Semantic Scholar estimates that this publication has 122 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Kato2004CommonMO, title={Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.}, author={Yusuke Kato and Koji Nagata and Mihoko Takahashi and Lubing Lian and Juan Antonio de Juan Herrero and Marius Sudol and Masaru Tanokura}, journal={The Journal of biological chemistry}, year={2004}, volume={279 30}, pages={31833-41} }