 SPRY Domain | |
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| Class:Other | |
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Structure:
“Structure of the SPRY domain of SSB-2”
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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.
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Examples of Proteins:
| SPRY proteins |
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Binding Partner |
| SSB1, SSB2, SSB-4 |  |
Par-4 |
RanBPM, RanBP10
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c-Met |
| Pyrin (Marenostrin) | |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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