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SPRY Domain

“Structure of the SPRY domain of SSB-2”

Domain binding and function:
The SPRY domain was originally discovered as a sequence-repeat in the dual-specificity kinase splA of Dictyostelium and rabbit ryanodine receptor.  The ~140 amino acid residue domain adopts a novel fold consisting of a β-sandwich structure formed by two four-stranded antiparallel β-sheets with a unique topology.  In combination with the B30.2 domain, these two domains adopt an immunoglobulin-like fold.  The SPRY of SSB-2 binds prostate apoptosis response protein-4 (Par-4), while the SPRY domains of RanBPM, RanBP10 and SSB-1 mediate interactions with MET.  Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.
Examples of Proteins: 
SPRY proteins
Binding Partner
SSB1, SSB2, SSB-4 Par-4
RanBPM, RanBP10   
Pyrin (Marenostrin)

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