Journal
PROTEIN SCIENCE
Volume 22, Issue 1, Pages 1-10Publisher
WILEY
DOI: 10.1002/pro.2185
Keywords
SPRY domain; PRY; B30; 2 domain; TRIM; BTN; SPSB; SOCS box; IgG; innate immunity; structure; function
Categories
Funding
- National Health and Medical Research Council (NHMRC), Australia [461219, 637348]
- NHMRC IRIISS [361646]
- NHMRC
- Australian Research Council [FT110100169]
- Australian Government
- Victorian State Government
- Australian Research Council [FT110100169] Funding Source: Australian Research Council
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The SPRY domain is a protein interaction module found in 77 murine and 100 human proteins, and is implicated in important biological pathways, including those that regulate innate and adaptive immunity. The current definition of the SPRY domain is based on a sequence repeat discovered in the splA kinase and ryanodine receptors. The greater SPRY family is divided into the B30.2 (which contains a PRY extension at the N-terminus) and SPRY-only sub-families. In this brief review, we examine the current structural and biochemical literature on SPRY/B30.2 domain involvement in key immune processes and highlight a PRY-like 60 amino acid region in the N-terminus of SPRY-only proteins. Phylogenetic, structural, and functional analyses suggest that this N-terminal region is related to the PRY region of B30.2 and should be characterized as part of an extended SPRY domain. Greater understanding of the functional importance of the N-terminal region in SPRY only proteins will enhance our ability to interrogate SPRY interactions with their respective binding partners.
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