2dyn
From Proteopedia
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'''DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)''' | '''DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Timm, D E.]] | [[Category: Timm, D E.]] | ||
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| - | [[Category: | + | [[Category: Protein binding]] |
| - | [[Category: | + | [[Category: Signal transduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:37:43 2008'' | |
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Revision as of 22:37, 3 May 2008
DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)
Overview
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.
About this Structure
2DYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 01:37:43 2008
