Exploring the diversity of SPRY/B30.2-mediated interactions

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• 作者：Livia Perfetto¹ ; ^* ; Pier Federico Gherardini¹ ; ^* ; Norman E. Davey³ ; Francesca Diella³ ; ⁴ ; Manuela Helmer-Citterich¹ ; Gianni Cesareni¹ ; ² ; ^{cesareni@uniroma2.it}
• 刊名：Trends in Biochemical Sciences
• 出版年：2013
• 出版时间：January, 2013
• 年：2013
• 卷：38
• 期：1
• 页码：38-46
• 全文大小：850 K

文摘

The SPla/Ryanodine receptor (SPRY)/B30.2 domain is one of the most common folds in higher eukaryotes. The human genome encodes 103 SPRY/B30.2 domains, several of which are involved in the immune response. Approximately 45 % of human SPRY/B30.2-containing proteins are E3 ligases. The role and function of the majority of SPRY/B30.2 domains are still poorly understood, however, in several cases mutations in this domain have been linked to congenital disorders. The recent characterization of SPRY/B30.2-mediated protein interactions has provided evidence for a role of this domain as an adaptor module to assemble macromolecular complexes, analogous to Src homology (SH)2, SH3, and WW domains. However, functional and structural evidence suggests that SPRY/B30.2 is a more versatile fold, allowing a wide range of binding modes.