View source for 2dyn

[[Image:2dyn.gif|left|200px]]

 {{Structure
|PDB= 2dyn |SIZE=350|CAPTION= <scene name='initialview01'>2dyn</scene>, resolution 2.30&Aring;
|SITE= 
|LIGAND= 
|ACTIVITY= 
|GENE= 
}}

'''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.

==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==
2DYN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DYN 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:[http://www.ncbi.nlm.nih.gov/pubmed/7634088 7634088]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Timm, D E.]]
[[Category: motor protein]]
[[Category: phospholipid binding]]
[[Category: protein binding]]
[[Category: signal transduction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:33:12 2008''