Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity

Akshay D'Cruz, Jeffrey Babon, Raymond Stanley Norton, Nicos A Nicola, Sandra E Nicholson

Research output: Contribution to journalArticleResearchpeer-review

63 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)1 - 10
Number of pages10
JournalProtein Science
Volume22
Issue number1
DOIs
Publication statusPublished - 2013

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