1edu
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(New page: 200px<br /><applet load="1edu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edu, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:48, 20 November 2007
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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 with EDO as ligand. 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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