publication . Other literature type . Article . 2013

Exploring the Diversity of SPRY/B30.2-mediated Interactions

Livia Perfetto; Pier Federico Gherardini; Norman E. Davey; Francesca Diella; Manuela Helmer-Citterich; Gianni Cesareni;
  • Published: 01 Jan 2013
  • Publisher: Elsevier BV
Abstract
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)...
Subjects
free text keywords: Biochemistry, Molecular Biology, Proto-oncogene tyrosine-protein kinase Src, Protein–protein interaction, Ryanodine receptor, Homology (biology), Cell biology, Signal transducing adaptor protein, Membrane protein, Genetics, Human genome, Biology, Protein structure
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