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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 with as ligand. 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

Page seeded by OCA on Thu Feb 21 12:26:43 2008

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OCA

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-[[Image:1edu.gif|left|200px]]<br /><applet load="1edu" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1edu, resolution 1.8&Aring;" />
 '''CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1'''<br />
 ==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.
+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==
-EDU 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EDU OCA].
+EDU 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==
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 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Brunger, A.T.]]
+[[Category: Brunger, A T.]]
 [[Category: Chen, H.]]
 [[Category: Decamilli, P.]]
-[[Category: Hyman, J.H.]]
+[[Category: Hyman, J H.]]
 [[Category: EDO]]
 [[Category: alpha-helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:55:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:43 2008''