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[[Image:1edu.gif|left|200px]] | [[Image:1edu.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1''' | {{Structure | ||
|PDB= 1edu |SIZE=350|CAPTION= <scene name='initialview01'>1edu</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EDU is a [ | 1EDU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDU OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10791968 10791968] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:54:13 2008'' | ||
Revision as of 08:54, 20 March 2008
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| 1edu, resolution 1.8Å | |||||||||||||
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| Ligands: | EDO | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1
Overview
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 Structure
1EDU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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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