The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization

@article{Stapleton1999TheCS,
  title={The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization},
  author={David I. Stapleton and I Balan and Tony Pawson and Frank Sicheri},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={44-49}
}
The sterile alpha motif (SAM) domain is a novel protein module of ~70 amino acids that is found in a variety of signaling molecules including tyrosine and serine/threonine protein kinases, cytoplasmic scaffolding and adaptor proteins, regulators of lipid metabolism, and GTPases as well as members of the ETS family of transcription factors. The SAM domain can potentially function as a protein interaction module through the ability to homo– and hetero–oligomerize with other SAM domains. This… 

Figures and Tables from this paper

Monomeric Structure of the Human EphB2 Sterile α Motif Domain*
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Coupled regulation by the juxtamembrane and sterile α motif (SAM) linker is a hallmark of ephrin tyrosine kinase evolution
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TLDR
The structure of the SLy1 SAM domain was solved and revealed that this SAM domain forms a symmetric homodimer through a novel interface, making the SLY1 SAM dimer two orders of magnitude more stable than previously studied SAM homodimers, suggesting that theSLy1SAM dimerization is of functional significance.
Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association.
TLDR
The structure of the SLy1 SAM domain was solved and revealed that this SAM domain forms a symmetric homodimer through a novel interface, making the SLY1 SAM dimer two orders of magnitude more stable than previously studied SAM homodimers, suggesting that theSLy1SAM dimerization is of functional significance.
Binding and Function of Phosphotyrosines of the Ephrin A2 (EphA2) Receptor Using Synthetic Sterile α Motif (SAM) Domains*
TLDR
It is shown that tyrosine phosphorylation of any of the three tyrosines, Tyr921, Tyr930, and Tyr960, has a surprisingly small effect on the EphA2 SAM structure and stability, however,osphorylation at Tyr 921 and Tyr930 enables differential binding to the Src homology 2 domain of the adaptor protein Grb7, which is proposed to lead to distinct functional outcomes.
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