2dyn
From Proteopedia
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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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:41:20 2008'' |
Revision as of 23:41, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:41:20 2008
