1edu
From Proteopedia
(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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| - | [[Image:1edu.gif|left|200px]]<br /><applet load="1edu" size=" | + | [[Image:1edu.gif|left|200px]]<br /><applet load="1edu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1edu, resolution 1.8Å" /> | caption="1edu, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1'''<br /> | '''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Epsin (Eps15 interactor) is a cytosolic protein involved in | + | 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== | ==About this Structure== | ||
| - | 1EDU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EDU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
[[Category: Chen, H.]] | [[Category: Chen, H.]] | ||
[[Category: Decamilli, P.]] | [[Category: Decamilli, P.]] | ||
| - | [[Category: Hyman, J | + | [[Category: Hyman, J H.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:43 2008'' |
Revision as of 10:26, 21 February 2008
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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 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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