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[[Image:1edu.gif|left|200px]]
{{Seed}}
[[Image:1edu.png|left|200px]]


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{{STRUCTURE_1edu|  PDB=1edu  |  SCENE=  }}  
{{STRUCTURE_1edu|  PDB=1edu  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1'''
===CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10791968}}


==About this Structure==
==About this Structure==
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[[Category: Hyman, J H.]]
[[Category: Hyman, J H.]]
[[Category: Alpha-helix]]
[[Category: Alpha-helix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:58:28 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:32:48 2008''

Revision as of 21:32, 30 June 2008

File:1edu.png

Template:STRUCTURE 1edu

CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1

Template:ABSTRACT PUBMED 10791968

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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