Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation.

@article{Owen1998CrystalSO,
  title={Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation.},
  author={David John Melvin Owen and Patrick Wigge and Yvonne Vallis and Jonathan D. Moore and Philip Rainsford Evans and Harvey T McMahon},
  journal={The EMBO journal},
  year={1998},
  volume={17 18},
  pages={
          5273-85
        }
}
The amphiphysins are brain-enriched proteins, implicated in clathrin-mediated endocytosis, that interact with dynamin through their SH3 domains. To elucidate the nature of this interaction, we have solved the crystal structure of the amphiphysin-2 (Amph2) SH3 domain to 2.2 A. The structure possesses several notable features, including an extensive patch of negative electrostatic potential covering a large portion of its dynamin binding site. This patch accounts for the specific requirement of… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 59 REFERENCES

A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 1996
VIEW 3 EXCERPTS
HIGHLY INFLUENTIAL

Methods used in the structure determination of bovine mitochondrial F1 ATPase.

  • Acta crystallographica. Section D, Biological crystallography
  • 1996
VIEW 2 EXCERPTS
HIGHLY INFLUENTIAL

Synergistic activation of dynamin GTPase by Grb2 and phosphoinositides

D ActaCrystallogr., B. 30–42. Barylko, +6 authors J. P. Albanesi
  • J . Biol . Chem .
  • 1998

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