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SAM Domain
Structure:

No Image 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.
 

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.
Examples of Proteins: 
SAM domain protein
Binding partner
Polycomb group chromatin remodelling proteins: Scm, ph, Rae28Homotypic and heterotypic interactions
Ste11 Yeast MAPKKK Ste50
Tel ETS family transcription factor

Tel

  Smaug                                                                                                RNA

No Image

 
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