Crystal structure of the pleckstrin homology domain from dynamin
- 1 November 1994
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 1 (11) , 782-788
- https://doi.org/10.1038/nsb1194-782
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.Keywords
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