title: 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 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.
authors.affiliation: Department of Crystallography, Birkbeck College, London, UK.
authors.forename: D
authors.initials: D
authors.lastname: Timm
authors.forename: K
authors.initials: K
authors.lastname: Salim
authors.forename: I
authors.initials: I
authors.lastname: Gout
authors.forename: L
authors.initials: L
authors.lastname: Guruprasad
authors.forename: M
authors.initials: M
authors.lastname: Waterfield
authors.forename: T
authors.initials: T
authors.lastname: Blundell
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry; D008969:Molecular Sequence Data; D010750:Phosphoproteins; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D001798:Blood Proteins; D010750:Phosphoproteins; C039077:platelet protein P47; D020558:GTP Phosphohydrolases; D034281:Dynamins