 SAM Domain | |
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Structure:
 Four different solved SAM domain structures reveal a compact 5 helix bundle with a conserved hydrophobic core. In the case of the SAM domains from EphA4 and EphB2, homotypic oligomerization was observed in the crystal structure, but the contact points that mediate self-association were found to be different. In contrast, the SAM domain of p73 was solved as a monomer. The monomeric form of the EphA4 SAM domain is shown.
Structure Reference:
Stapleton, D. et al. (1999) Nat. Struct. Biol. 6(1):44-9. PDB: 1B0X.
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Domain binding and function:
The approximately 70 amino acid SAM (Sterile Alpha Motif) domain has been identified in over 400 different proteins with diverse cellular function, from yeast to man. SAM domains have been implicated in mediating protein-protein interaction via the formation of homo and hetero-typic oligomers. The residues at the interface of the EphA4 and EphB2 SAM domain homodimers have been mapped, but the factors that determine specificity remain to be determined. | |
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| Examples of Proteins: Smaug RNA |
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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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