2dyn

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{{STRUCTURE_2dyn| PDB=2dyn | SCENE= }}
{{STRUCTURE_2dyn| PDB=2dyn | SCENE= }}
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'''DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)'''
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===DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7634088 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7634088}}
==About this Structure==
==About this Structure==
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[[Category: Protein binding]]
[[Category: Protein binding]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:35:28 2008''

Revision as of 13:35, 27 July 2008

Template:STRUCTURE 2dyn

DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)

Template:ABSTRACT PUBMED 7634088

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

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