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… 
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Monomeric Structure of the Human EphB2 Sterile α Motif Domain*
TLDR
A new crystal form of the human EphB2-SAM domain is solved that has the same overall SAM domain fold yet has no substantial intermolecular contacts and suggests that Tyr-8 is not part of the hydrophobic core of the Eph B2- SAM domain and is conserved for functional reasons.
Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites
TLDR
A highly conserved subclass of SAM domains is present at the intracellular C‐terminus of more than 40 Eph receptor tyrosine kinases that are involved in the control of axonal pathfinding upon ephrin‐induced oligomerization and activation in the event of cell‐cell contacts.
Solution structure of a conserved C‐terminal domain of p73 with structural homology to the SAM domain
TLDR
The three‐dimensional solution structure of this conserved C‐terminal domain of human p73 reveals a small five‐helix bundle with striking similarity to the SAM (sterile alpha motif) domains of two ephrin receptor tyrosine kinases, suggesting that this domain may interact with additional, as yet uncharacterized proteins in a signaling and/or regulatory role.
The SAM domain inhibits EphA2 interactions in the plasma membrane.
Coupled regulation by the juxtamembrane and sterile α motif (SAM) linker is a hallmark of ephrin tyrosine kinase evolution
TLDR
It is reported for the first time that the SAM domain linker is functionally coupled to the juxtamembrane through co-conserved residues in the kinase domain and that together these residues provide a structural framework for coupling catalytic and regulatory functions.
Systematic biochemical characterization of the SAM domains in Eph receptor family from Mus Musculus.
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.
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.
Structural Basis for Autoinhibition of the EphB2 Receptor Tyrosine Kinase by the Unphosphorylated Juxtamembrane Region
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