CRYSTAL-STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DYNAMIN

The pleckstrin homology (PH) domain is a conserved module present in m any signal transducing and cytoskeletal proteins. Here we report the 2 .8 Angstrom crystal structure of the PH domain from dynamin. This doma in consists of seven beta-strands forming two roughly orthogonal antip arallel beta-sheets terminating with an amphipathic alpha-helix. The s tructure also reveals a non-covalent dimeric association of the PH dom ain 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.