5lp0: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5lp0" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF THE ZEBRA FISH ENTH DOMAIN FROM EPSIN1 IN 1.41 ANGSTROM RESOLUTION== | |||
<StructureSection load='5lp0' size='340' side='right' caption='[[5lp0]], [[Resolution|resolution]] 1.41Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lp0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LP0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h0a|1h0a]], [[1edu|1edu]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lp0 OCA], [http://pdbe.org/5lp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lp0 RCSB], [http://www.ebi.ac.uk/pdbsum/5lp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lp0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 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<ref>PMID:10791968</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5lp0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Levin-Kravets, O]] | |||
[[Category: Prag, G]] | [[Category: Prag, G]] | ||
[[Category: | [[Category: Alpha-helix]] | ||
[[Category: Endocytosis membrane assembly]] | |||
[[Category: Intracellular membrane trafficking]] | |||
[[Category: Signaling protein]] | |||
[[Category: Ubiquitin-binding protein]] | |||
