| Literature DB >> 7634088 |
D Timm1, K Salim, I Gout, L Guruprasad, M Waterfield, T Blundell.
Abstract
The pleckstrin homology (PH) domain is a conserved module present in many signal transducing and cytoskeletal proteins. Here we report the 2.8 A crystal structure of the PH domain from dynamin. This domain consists of seven beta-strands forming two roughly orthogonal antiparallel beta-sheets terminating with an amphipathic alpha-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.Mesh:
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Year: 1994 PMID: 7634088 DOI: 10.1038/nsb1194-782
Source DB: PubMed Journal: Nat Struct Biol ISSN: 1072-8368