Crystal structure of the pleckstrin homology domain from dynamin

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. © 1994 Nature Publishing group.