Kofler Michael M, Freund Christian
Protein Engineering Group, Free University and FMP Berlin, Germany.
FEBS J. 2006 Jan;273(2):245-56. doi: 10.1111/j.1742-4658.2005.05078.x.
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.
GYF结构域是一类小的、多功能的衔接子结构域，可识别富含脯氨酸的序列（PRS）。它们存在于目前已测序的大多数真核生物物种中，但与其他PRS识别结构域（PRD）不同的是，GYF结构域在后生动物进化过程中并未经历同样的扩增。突变和结构分析表明，保守序列W-X-Y-X(6-11)-GPF-X(4)-M-X(2)-W-X(3)-GYF是与富含脯氨酸肽段相互作用的位点。相比之下，GYF结构域C端的组成和长度并不保守。与其他PRD类似，GYF结构域可与许多不同的PRS结合，这些PRS汇聚于一个最小共有序列。目前分析的所有GYF结构域都选择了核心基序PPG，而该基序相邻的氨基酸偏好各不相同。基于此分析，已鉴定出两个亚家族：CD2BP2型和SMY2型GYF结构域。后一个亚家族包含大多数GYF结构域，其特征是β(1)-β(2)环较短，且在第8位有一个天冬氨酸，而非CD2BP2型GYF结构域中的色氨酸。最近对GYF结构域结合特异性的分析使得鉴定出新的相互作用伙伴成为可能。蛋白质组学由此有助于从功能上理解含GYF结构域的蛋白质，并为更系统地研究它们在体内的功能奠定了基础。
