Crystal structure of the pleckstrin homology domain from dynamin
Crystal structure of the pleckstrin homology domain from dynamin
| dc.contributor.author | Timm, David | |
| dc.contributor.author | Salim, Kamran | |
| dc.contributor.author | Gout, Ivan | |
| dc.contributor.author | Guruprasad, Lalitha | |
| dc.contributor.author | Waterfield, Mike | |
| dc.contributor.author | Blundell, Tom | |
| dc.date.accessioned | 2022-03-27T08:34:05Z | |
| dc.date.available | 2022-03-27T08:34:05Z | |
| dc.date.issued | 1994-01-01 | |
| dc.description.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. | |
| dc.identifier.citation | Nature Structural Biology. v.1(11) | |
| dc.identifier.issn | 10728368 | |
| dc.identifier.uri | 10.1038/nsb1194-782 | |
| dc.identifier.uri | http://www.nature.com/doifinder/10.1038/nsb1194-782 | |
| dc.identifier.uri | https://dspace.uohyd.ac.in/handle/1/10865 | |
| dc.title | Crystal structure of the pleckstrin homology domain from dynamin | |
| dc.type | Journal. Article | |
| dspace.entity.type |
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