2kfg
From Proteopedia
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==Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK== | ==Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK== | ||
| - | <StructureSection load='2kfg' size='340' side='right'caption='[[2kfg | + | <StructureSection load='2kfg' size='340' side='right'caption='[[2kfg]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2kfg]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2kfg]] is a 2 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=2KFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KFG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfg OCA], [https://pdbe.org/2kfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kfg RCSB], [https://www.ebi.ac.uk/pdbsum/2kfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kfg ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/EHD1_HUMAN EHD1_HUMAN] Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes.<ref>PMID:15020713</ref> <ref>PMID:17233914</ref> |
== 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=2kfg 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=2kfg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues. | ||
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| - | Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.,Kieken F, Jovic M, Tonelli M, Naslavsky N, Caplan S, Sorgen PL Protein Sci. 2009 Dec;18(12):2471-9. PMID:19798736<ref>PMID:19798736</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2kfg" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Caplan | + | [[Category: Caplan S]] |
| - | [[Category: Jovic | + | [[Category: Jovic M]] |
| - | [[Category: Kieken | + | [[Category: Kieken F]] |
| - | [[Category: Naslavsky | + | [[Category: Naslavsky N]] |
| - | [[Category: Sorgen | + | [[Category: Sorgen P]] |
| - | [[Category: Tonelli | + | [[Category: Tonelli M]] |
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Current revision
Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK
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Categories: Homo sapiens | Large Structures | Caplan S | Jovic M | Kieken F | Naslavsky N | Sorgen P | Tonelli M
