title: The GYF domain.
abstract: GYF domains are small, versatile adaptor domains that recognize proline-rich sequences (PRS). They are present in most eukaryotic species sequenced so far, but in contrast to other PRS-recognition domains (PRD), GYF domains have not experienced the same amplification in metazoa during evolution. Mutational and structural analysis has shown the conserved signature W-X-Y-X(6-11)-GPF-X(4)-M-X(2)-W-X(3)-GYF to be the site of interaction with proline-rich peptides. In contrast, composition and length of the C-terminal half of GYF domains are not conserved. Similar to other PRD, GYF domains bind to many different PRS that converge on a minimal consensus sequence. All GYF domains analyzed so far selected for the core motif PPG, whereas amino-acid preferences adjacent to this motif vary. As a result of this analysis, two subfamilies have been identified: CD2BP2-type and SMY2-type GYF domains. The latter subfamily comprises most GYF domains and is characterized by a shorter beta(1)-beta(2) loop and an aspartate instead of the tryptophan found at position 8 in CD2BP2-type GYF domains. Recent analysis of binding specificities for GYF domains allowed identification of novel interaction partners. Thereby proteomics has contributed to a functional understanding of GYF domain-containing proteins and sets the stage for a more systematic investigation of their functions in vivo.
authors.affiliation: Protein Engineering Group, Free University and FMP Berlin, Germany. kofler@fmp-berlin.de
authors.forename: Michael M
authors.initials: MM
authors.lastname: Kofler
authors.forename: Christian
authors.initials: C
authors.lastname: Freund
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D008024:Ligands; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D055232:Proline-Rich Protein Domains; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
chemical_list: D008024:Ligands; D010455:Peptides