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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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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DOI: https://doi.org/10.1038/nsb1194-782
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