1edu: Difference between revisions

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|PDB= 1edu |SIZE=350|CAPTION= <scene name='initialview01'>1edu</scene>, resolution 1.8&Aring;
|PDB= 1edu |SIZE=350|CAPTION= <scene name='initialview01'>1edu</scene>, resolution 1.8&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edu OCA], [http://www.ebi.ac.uk/pdbsum/1edu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1edu RCSB]</span>
}}
}}


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[[Category: Decamilli, P.]]
[[Category: Decamilli, P.]]
[[Category: Hyman, J H.]]
[[Category: Hyman, J H.]]
[[Category: EDO]]
[[Category: alpha-helix]]
[[Category: alpha-helix]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:32 2008''

Revision as of 20:00, 30 March 2008

File:1edu.gif


PDB ID 1edu

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1


OverviewOverview

Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1- dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function.

About this StructureAbout this Structure

1EDU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)., Hyman J, Chen H, Di Fiore PP, De Camilli P, Brunger AT, J Cell Biol. 2000 May 1;149(3):537-46. PMID:10791968

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