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| | ==SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN== | | ==SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN== |
| - | <StructureSection load='1inz' size='340' side='right'caption='[[1inz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1inz' size='340' side='right'caption='[[1inz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1inz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1INZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1inz]] 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=1INZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1INZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1inz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inz OCA], [http://pdbe.org/1inz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1inz RCSB], [http://www.ebi.ac.uk/pdbsum/1inz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1inz ProSAT], [http://www.topsan.org/Proteins/RSGI/1inz TOPSAN]</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=1inz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inz OCA], [https://pdbe.org/1inz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1inz RCSB], [https://www.ebi.ac.uk/pdbsum/1inz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1inz ProSAT], [https://www.topsan.org/Proteins/RSGI/1inz TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EPN1_HUMAN EPN1_HUMAN]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.<ref>PMID:10557078</ref> | + | [https://www.uniprot.org/uniprot/EPN1_HUMAN EPN1_HUMAN] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.<ref>PMID:10557078</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: Kigawa, T]] | + | [[Category: Kigawa T]] |
| - | [[Category: Kikuchi, A]] | + | [[Category: Kikuchi A]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Koshiba S]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Alpha-helix]]
| + | |
| - | [[Category: Endocytosis-exocytosis complex]]
| + | |
| - | [[Category: Epsin]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
EPN1_HUMAN Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.[1]
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
Epsin is a protein that binds to the Eps15 homology (EH) domains, and is involved in clathrin-mediated endocytosis. The epsin N-terminal homology (ENTH) domain (about 140 amino acid residues) is well conserved in eukaryotes and is considered to be important for actin cytoskeleton organization in endocytosis. In this study, we have determined the solution structure of the ENTH domain (residues 1-144) of human epsin by multidimensional nuclear magnetic resonance spectroscopy. In the ENTH-domain structure, seven alpha-helices form a superhelical fold, consisting of two antiparallel two-helix HEAT motifs and one three-helix ARM motif, with a continuous hydrophobic core in the center. We conclude that the seven-helix superhelical fold defines the ENTH domain, and that the previously-reported eight-helix fold of a longer fragment of rat epsin 1 is divided into the authentic ENTH domain and a C-terminal flanking alpha-helix.
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin.,Koshiba S, Kigawa T, Kikuchi A, Yokoyama S J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morinaka K, Koyama S, Nakashima S, Hinoi T, Okawa K, Iwamatsu A, Kikuchi A. Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis. Oncogene. 1999 Oct 21;18(43):5915-22. PMID:10557078 doi:http://dx.doi.org/10.1038/sj.onc.1202974
- ↑ Koshiba S, Kigawa T, Kikuchi A, Yokoyama S. Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin. J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669
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