2dyn: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyn OCA], [http://www.ebi.ac.uk/pdbsum/2dyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dyn RCSB]</span>
}}
}}


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==Overview==
==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.
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.
==Disease==
Known diseases associated with this structure: Encephalopahty, lethal, due to defective mitochondrial peroxisomal fission OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603850 603850]]


==About this Structure==
==About this Structure==
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[[Category: signal transduction]]
[[Category: signal transduction]]


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