4gjt
From Proteopedia
(Difference between revisions)
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| - | + | ==complex structure of nectin-4 bound to MV-H== | |
| - | + | <StructureSection load='4gjt' size='340' side='right' caption='[[4gjt]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4gjt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Measles_virus_strain_ichinose-b95a Measles virus strain ichinose-b95a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GJT FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rkc|2rkc]], [[2zb5|2zb5]], [[3alw|3alw]], [[3inb|3inb]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H, hemagglutinin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=645098 Measles virus strain Ichinose-B95a]), LNIR, nectin-4, PRR4, PVRL4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gjt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gjt RCSB], [http://www.ebi.ac.uk/pdbsum/4gjt PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/PVRL4_HUMAN PVRL4_HUMAN]] Ectodermal dysplasia - syndactyly syndrome. Defects in PVRL4 are the cause of ectodermal dysplasia-syndactyly syndrome type 1 (EDSS1) [MIM:[http://omim.org/entry/613573 613573]]. EDSS1 is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSS1 is characterized by the association of hair and teeth abnormalities with cutaneous syndactyly of the hands and/or feet. Hair morphologic abnormalities include twists at irregular intervals (pilli torti) and swelling along the shafts, particularly associated with areas of breakage. Dental findings consist of abnormally widely spaced teeth, with peg-shaped and conical crowns. Patients have normal sweating.<ref>PMID:20691405</ref> | [[http://www.uniprot.org/uniprot/PVRL4_HUMAN PVRL4_HUMAN]] Ectodermal dysplasia - syndactyly syndrome. Defects in PVRL4 are the cause of ectodermal dysplasia-syndactyly syndrome type 1 (EDSS1) [MIM:[http://omim.org/entry/613573 613573]]. EDSS1 is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSS1 is characterized by the association of hair and teeth abnormalities with cutaneous syndactyly of the hands and/or feet. Hair morphologic abnormalities include twists at irregular intervals (pilli torti) and swelling along the shafts, particularly associated with areas of breakage. Dental findings consist of abnormally widely spaced teeth, with peg-shaped and conical crowns. Patients have normal sweating.<ref>PMID:20691405</ref> | ||
| - | + | == Function == | |
| - | ==Function== | + | |
[[http://www.uniprot.org/uniprot/HEMA_MEASC HEMA_MEASC]] Attaches the virus to cell receptors and thereby initiating infection. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion. May use human CD46 and/or SLAMF1 as receptors for viral entry into the cell. The high degree of interaction between H and MCP/CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis (By similarity). [[http://www.uniprot.org/uniprot/PVRL4_HUMAN PVRL4_HUMAN]] Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells. | [[http://www.uniprot.org/uniprot/HEMA_MEASC HEMA_MEASC]] Attaches the virus to cell receptors and thereby initiating infection. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion. May use human CD46 and/or SLAMF1 as receptors for viral entry into the cell. The high degree of interaction between H and MCP/CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis (By similarity). [[http://www.uniprot.org/uniprot/PVRL4_HUMAN PVRL4_HUMAN]] Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Measles virus is a major public health concern worldwide. Three measles virus cell receptors have been identified so far, and the structures of the first two in complex with measles virus hemagglutinin (MV-H) have been reported. Nectin-4 is the most recently identified receptor in epithelial cells, and its binding mode to MV-H remains elusive. In this study, we solved the structure of the membrane-distal domain of human nectin-4 in complex with MV-H. The structure shows that nectin-4 binds the MV-H beta4-beta5 groove exclusively via its N-terminal IgV domain; the contact interface is dominated by hydrophobic interactions. The binding site in MV-H for nectin-4 also overlaps extensively with those of the other two receptors. Finally, a hydrophobic pocket centered in the beta4-beta5 groove is involved in binding to all three identified measles virus receptors, representing a potential target for antiviral drugs. | ||
| - | + | Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.,Zhang X, Lu G, Qi J, Li Y, He Y, Xu X, Shi J, Zhang CW, Yan J, Gao GF Nat Struct Mol Biol. 2013 Jan;20(1):67-72. doi: 10.1038/nsmb.2432. Epub 2012 Dec , 2. PMID:23202587<ref>PMID:23202587</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <references | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Measles virus strain ichinose-b95a]] | [[Category: Measles virus strain ichinose-b95a]] | ||
| - | [[Category: Gao, G F | + | [[Category: Gao, G F]] |
| - | [[Category: He, Y | + | [[Category: He, Y]] |
| - | [[Category: Li, Y | + | [[Category: Li, Y]] |
| - | [[Category: Lu, G | + | [[Category: Lu, G]] |
| - | [[Category: Qi, J | + | [[Category: Qi, J]] |
| - | [[Category: Shi, J | + | [[Category: Shi, J]] |
| - | [[Category: Xu, X | + | [[Category: Xu, X]] |
| - | [[Category: Yan, J | + | [[Category: Yan, J]] |
| - | [[Category: Zhang, C | + | [[Category: Zhang, C]] |
| - | [[Category: Zhang, X | + | [[Category: Zhang, X]] |
[[Category: Beta4/beta5 groove]] | [[Category: Beta4/beta5 groove]] | ||
[[Category: Igv-like fold]] | [[Category: Igv-like fold]] | ||
Revision as of 11:06, 21 December 2014
complex structure of nectin-4 bound to MV-H
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