1h0a

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[[Image:1h0a.jpg|left|200px]]
 
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{{Structure
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==Epsin ENTH bound to Ins(1,4,5)P3==
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|PDB= 1h0a |SIZE=350|CAPTION= <scene name='initialview01'>1h0a</scene>, resolution 1.70&Aring;
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<StructureSection load='1h0a' size='340' side='right'caption='[[1h0a]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE= <scene name='pdbsite=DI1:I3p+Binding+Site+For+Chain+A'>DI1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene> and <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE=
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<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>
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}}
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/1h0a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h0a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''EPSIN ENTH BOUND TO INS(1,4,5)P3'''
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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<ref>PMID:12353027</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1h0a" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Epsin|Epsin]]
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== References ==
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==About this Structure==
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<references/>
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1H0A is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12353027 12353027]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Evans PR]]
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[[Category: Evans, P R.]]
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[[Category: Ford MGJ]]
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[[Category: Ford, M G.J.]]
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[[Category: McMahon HT]]
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[[Category: Mcmahon, H T.]]
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[[Category: DIO]]
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[[Category: I3P]]
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[[Category: 4]]
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[[Category: 5)p3]]
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[[Category: alpha-alpha superhelix]]
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[[Category: clathrin]]
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[[Category: coated vesicle]]
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[[Category: endocytosis]]
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[[Category: enth]]
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[[Category: epsin]]
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[[Category: ins(1]]
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[[Category: triskelion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:31 2008''
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Current revision

Epsin ENTH bound to Ins(1,4,5)P3

PDB ID 1h0a

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