Crystal structure of the pleckstrin homology domain from dynamin.
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.
Timm
D
D
Department of Crystallography, Birkbeck College, London, UK.
Salim
K
K
Gout
I
I
Guruprasad
L
L
Waterfield
M
M
Blundell
T
T
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
D001798:Blood Proteins; D010750:Phosphoproteins; C039077:platelet protein P47; D020558:GTP Phosphohydrolases; D034281:Dynamins