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.