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| | <StructureSection load='1h0a' size='340' side='right'caption='[[1h0a]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1h0a' size='340' side='right'caption='[[1h0a]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H0A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H0A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1edu|1edu]], [[1eyh|1eyh]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0a OCA], [https://pdbe.org/1h0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h0a RCSB], [https://www.ebi.ac.uk/pdbsum/1h0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0a ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0a OCA], [https://pdbe.org/1h0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h0a RCSB], [https://www.ebi.ac.uk/pdbsum/1h0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>
| + | [https://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Evans, P R]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Ford, M G.J]] | + | [[Category: Evans PR]] |
| - | [[Category: McMahon, H T]] | + | [[Category: Ford MGJ]] |
| - | [[Category: Alpha-alpha superhelix]] | + | [[Category: McMahon HT]] |
| - | [[Category: Clathrin]]
| + | |
| - | [[Category: Coated vesicle]]
| + | |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: Enth]]
| + | |
| - | [[Category: Epsin]]
| + | |
| - | [[Category: Triskelion]]
| + | |
| Structural highlights
Function
EPN1_RAT Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Clathrin-mediated endocytosis involves cargo selection and membrane budding into vesicles with the aid of a protein coat. Formation of invaginated pits on the plasma membrane and subsequent budding of vesicles is an energetically demanding process that involves the cooperation of clathrin with many different proteins. Here we investigate the role of the brain-enriched protein epsin 1 in this process. Epsin is targeted to areas of endocytosis by binding the membrane lipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)). We show here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P(2) in conjunction with clathrin polymerization. We have discovered that formation of an amphipathic alpha-helix in epsin is coupled to PtdIns(4,5)P(2) binding. Mutation of residues on the hydrophobic region of this helix abolishes the ability to curve membranes. We propose that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature. On lipid monolayers epsin alone is sufficient to facilitate the formation of clathrin-coated invaginations.
Curvature of clathrin-coated pits driven by epsin.,Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature. 1998 Aug 20;394(6695):793-7. PMID:9723620 doi:http://dx.doi.org/10.1038/29555
- ↑ Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 2001 Feb 9;291(5506):1047-51. PMID:11161217 doi:http://dx.doi.org/10.1126/science.291.5506.1047
- ↑ Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. Curvature of clathrin-coated pits driven by epsin. Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027 doi:10.1038/nature01020
- ↑ Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. Curvature of clathrin-coated pits driven by epsin. Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027 doi:10.1038/nature01020
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