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| | ==Structure of EH-domain of EHD1== | | ==Structure of EH-domain of EHD1== |
| - | <StructureSection load='2jq6' size='340' side='right'caption='[[2jq6]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2jq6' size='340' side='right'caption='[[2jq6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jq6]] 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=2JQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jq6]] 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=2JQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQ6 FirstGlance]. <br> |
| - | </td></tr><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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHD1, PAST, PAST1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <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=2jq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jq6 OCA], [https://pdbe.org/2jq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jq6 RCSB], [https://www.ebi.ac.uk/pdbsum/2jq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jq6 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=2jq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jq6 OCA], [https://pdbe.org/2jq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jq6 RCSB], [https://www.ebi.ac.uk/pdbsum/2jq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jq6 ProSAT]</span></td></tr> |
| | </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>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Caplan, S]] | + | [[Category: Caplan S]] |
| - | [[Category: Jovic, M]] | + | [[Category: Jovic M]] |
| - | [[Category: Kieken, F P]] | + | [[Category: Kieken FP]] |
| - | [[Category: Sorgen, P L]] | + | [[Category: Sorgen PL]] |
| - | [[Category: Eh domain]]
| + | |
| - | [[Category: Ehd-1]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
EHD1_HUMAN Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes.[1] [2]
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
EHD1 is a member of the mammalian C-terminal Eps15 homology domain (EH) containing protein family, and regulates the recycling of various receptors from the endocytic recycling compartment to the plasma membrane. The EH domain of EHD1 binds to proteins containing either an Asn-Pro-Phe or Asp-Pro-Phe motif, and plays an important role in the subcellular localization and function of EHD1. Thus far, the structures of five N-terminal EH domains from other proteins have been solved, but to date, the structure of the EH domains from the four C-terminal EHD family paralogs remains unknown. In this study, we have assigned the 133 C-terminal residues of EHD1, which includes the EH domain, and solved its solution structure. While the overall structure resembles that of the second of the three N-terminal Eps15 EH domains, potentially significant differences in surface charge and the structure of the tripeptide-binding pocket are discussed.
EH domain of EHD1.,Kieken F, Jovic M, Naslavsky N, Caplan S, Sorgen PL J Biomol NMR. 2007 Dec;39(4):323-9. Epub 2007 Sep 26. PMID:17899392[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Naslavsky N, Boehm M, Backlund PS Jr, Caplan S. Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane. Mol Biol Cell. 2004 May;15(5):2410-22. Epub 2004 Mar 12. PMID:15020713 doi:http://dx.doi.org/10.1091/mbc.E03-10-0733
- ↑ George M, Ying G, Rainey MA, Solomon A, Parikh PT, Gao Q, Band V, Band H. Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans. BMC Cell Biol. 2007 Jan 18;8:3. PMID:17233914 doi:http://dx.doi.org/10.1186/1471-2121-8-3
- ↑ Kieken F, Jovic M, Naslavsky N, Caplan S, Sorgen PL. EH domain of EHD1. J Biomol NMR. 2007 Dec;39(4):323-9. Epub 2007 Sep 26. PMID:17899392 doi:10.1007/s10858-007-9196-0
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