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.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Blood Proteins, Computer Graphics, Crystallography, X-Ray, Dynamins, GTP Phosphohydrolases, Microtubules, Molecular Sequence Data, Phosphoproteins, Protein Conformation, Sequence Homology, Amino Acid
Amino Acid Sequence, Binding Sites, Blood Proteins, Computer Graphics, Crystallography, X-Ray, Dynamins, GTP Phosphohydrolases, Microtubules, Molecular Sequence Data, Phosphoproteins, Protein Conformation, Sequence Homology, Amino Acid
Nat. Struct. Biol.
Date: Nov. 01, 1994
PubMed ID: 7634088
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