Structural highlights
Function
[DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the pleckstrin homology domain from dynamin.,Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T Nat Struct Biol. 1994 Nov;1(11):782-8. PMID:7634088[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T. Crystal structure of the pleckstrin homology domain from dynamin. Nat Struct Biol. 1994 Nov;1(11):782-8. PMID:7634088
