|PROSITE documentation PDOC50188|
The B30.2 domain was first identified as a protein domain encoded by an exon (named B30-2) in the human class I major histocompatibility complex region , whereas the SPRY domain was first identified in a Dictyostelium discoideum kinase splA and mammalian calcium-release channels ryanodine receptors . The SPRY domains are shorter at the N-terminus than the B30.2 domains and appear as a subdomain of the latter. The ~200-residue B30.2/SPRY (for B30.2 and/or SPRY) domain is present in a large number of proteins with diverse individual functions in different biological processes. The B30.2/SPRY domain in these proteins is likely to function through protein-protein interaction .
The N-terminal ~60 residues of B30.2/SPRY domains are poorly conserved and, as a consequence, a new domain name PRY was coined for a group of similar sequence segments N-terminal to the SPRY domains . The B30.2/SPRY domain contains three highly conserved motifs (LDP, WEVE and LDYE) . The B30.2/SPRY domain adopts a highly distorted, compact β-sandwich fold with two additional short α-helices at the N-terminus (see <PDB:2FNJ>). The β-sandwich of the B30.2/SPRY domain consists of two layers of β-sheets: sheet A composed of eight strands and sheet B composed of seven strands. All the β-strands are in antiparallel arrangement . The 5th β-strand corresponding to WEVE motif . Both the N- and C-terminal ends of the B30.2/SPRY domains in general are close to each other .
Some proteins known to contain a B30.2/SPRY domain are listed below:
The profile we developed covers the entire B30.2/SPRY domain.Last update:
April 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Vernet C. Boretto J. Mattei M.G. Takahashi M. Jack L.J. Mather I.H. Rouquier S. Pontarotti P.|
|Title||Evolutionary study of multigenic families mapping close to the human MHC class I region.|
|Source||J. Mol. Evol. 37:600-612(1993).|
|2||Authors||Ponting C. Schultz J. Bork P.|
|Title||SPRY domains in ryanodine receptors (Ca(2+)-release channels).|
|Source||Trends Biochem. Sci. 22:193-194(1997).|
|3||Authors||Woo J.-S. Imm J.-H. Min C.-K. Kim K.-J. Cha S.-S. Oh B.-H.|
|Title||Structural and functional insights into the B30.2/SPRY domain.|
|Source||EMBO J. 25:1353-1363(2006).|
|4||Authors||Henry J. Ribouchon M.-T. Offer C. Pontarotti P.|
|Title||B30.2-like domain proteins: a growing family.|
|Source||Biochem. Biophys. Res. Commun. 235:162-165(1997).|
|5||Authors||Seto M.H. Liu H.-L.C. Zajchowski D.A. Whitlow M.|
|Title||Protein fold analysis of the B30.2-like domain.|