IPR003877
SPRY domain
InterPro entry
Short name | SPRY_dom |
Overlapping homologous superfamilies | |
domain relationships |
Description
The SPRY domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development
[3, 2, 4]. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region
[2]. SPRY/B30.2 structures revealed a bent β-sandwich fold comprised of two β-sheets. The PRY domain consists of three β-strands tightly packed against ten other β-strands which form the SPRY component of the B30.2 domain. The β-strands are linked by loops and form two anti-parallel β-sheets
[2]. Distant homologues are domains in butyrophilin/marenostrin/pyrin
[1].
References
1.SPRY domains in ryanodine receptors (Ca(2+)-release channels). Ponting C, Schultz J, Bork P. Trends Biochem. Sci. 22, 193-4, (1997). View articlePMID: 9204703
2.Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity. D'Cruz AA, Babon JJ, Norton RS, Nicola NA, Nicholson SE. Protein Sci. 22, 1-10, (2013). View articlePMID: 23139046
3.Structural basis for protein recognition by B30.2/SPRY domains. Woo JS, Suh HY, Park SY, Oh BH. Mol. Cell 24, 967-76, (2006). View articlePMID: 17189197
GO terms
Cross References
Representative structure
4qt6: Crystal structure of the SPRY domain of human HERC1