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Crystal structure of the pleckstrin homology domain from dynamin

Nature Structural Biology volume 1, pages 782–788 (1994)Cite this article

Abstract

The pleckstrin homology (PH) domain is a conserved module present in many signal transducing and cytoskeletal proteins. Here we report the 2.8 Å crystal structure of the PH domain from dynamin. This domain consists of seven β-strands forming two roughly orthogonal antiparallel β-sheets terminating with an amphipathic α-helix. The structure also reveals a non-covalent dimeric association of the PH domain and a hydrophobic pocket surrounded by a charged rim. The dynamin PH domain structure is discussed in relation to its potential role in mediating interactions between proteins.

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Authors and Affiliations

  1. ICRF Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK

    David Timm, Lalitha Guruprasad & Tom Blundell

  2. Ludwig Institute for Cancer Research, 91 Riding House Street, London, WC1E 8BP, UK

    Kamran Salim, Ivan Gout & Mike Waterfield

  3. Department of Biochemistry and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, UK

    Mike Waterfield

Authors
  1. David Timm
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  2. Kamran Salim
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  3. Ivan Gout
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  4. Lalitha Guruprasad
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  5. Mike Waterfield
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  6. Tom Blundell
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Timm, D., Salim, K., Gout, I. et al. Crystal structure of the pleckstrin homology domain from dynamin. Nat Struct Mol Biol 1, 782–788 (1994). https://doi.org/10.1038/nsb1194-782

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