TAILIEUCHUNG - Báo cáo khoa học: The GYF domain

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. | FEBS Journal REVIEW ARTICLE The GYF domain Michael M. Kofler and Christian Freund Protein Engineering Group Free University and FMP Berlin Germany Keywords adaptor domains function GYF domains interaction partners proline-rich sequences proline-rich sequence-recognition domains Correspondence M. M. Kotler C. Freund Protein Engineering Group Free University and FMP Berlin Robert-Rossle-Str. 10 13125 Berlin Germany Fax 49 30 94793 189 Tel 49 30 94793 181 E-mail freund@ kofler@ Received 6 October 2005 accepted 24 November 2005 doi GYF domains are small versatile adaptor domains that recognize prolinerich 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-X6-11-GPF-X4-M-X2-W-X3-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 P1-P2 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 domaincontaining proteins and sets the stage for a more systematic investigation of their functions in vivo. Structural elucidation of a GYF-ligand complex .

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