1hyj

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==SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN==
==SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN==
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<StructureSection load='1hyj' size='340' side='right'caption='[[1hyj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1hyj' size='340' side='right'caption='[[1hyj]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1hyj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1hyj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hyi|1hyi]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1hyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyj OCA], [https://pdbe.org/1hyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyj RCSB], [https://www.ebi.ac.uk/pdbsum/1hyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyj 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=1hyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyj OCA], [https://pdbe.org/1hyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyj RCSB], [https://www.ebi.ac.uk/pdbsum/1hyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/EEA1_HUMAN EEA1_HUMAN]] Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
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[https://www.uniprot.org/uniprot/EEA1_HUMAN EEA1_HUMAN] Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1hyj ConSurf].
</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=1hyj ConSurf].
<div style="clear:both"></div>
<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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The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.
 
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Structural mechanism of endosome docking by the FYVE domain.,Kutateladze T, Overduin M Science. 2001 Mar 2;291(5509):1793-6. PMID:11230696<ref>PMID:11230696</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 1hyj" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kutateladze, T]]
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[[Category: Kutateladze T]]
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[[Category: Overduin, M]]
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[[Category: Overduin M]]
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[[Category: Alpha helix]]
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[[Category: Beta sheet]]
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[[Category: Endocytosis-exocytosis complex]]
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[[Category: Zinc cluster]]
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Revision as of 07:43, 3 April 2024

SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN

PDB ID 1hyj

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