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| | ==Crystal structure of human nectin-4 extracellular fragment D1-D2== | | ==Crystal structure of human nectin-4 extracellular fragment D1-D2== |
| - | <StructureSection load='4frw' size='340' side='right' caption='[[4frw]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='4frw' size='340' side='right'caption='[[4frw]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4frw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FRW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4frw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FRW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fmf|4fmf]], [[4fmk|4fmk]], [[4fn0|4fn0]], [[4fom|4fom]], [[4fqp|4fqp]], [[4fs0|4fs0]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PVRL4, LNIR, PRR4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4frw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4frw OCA], [https://pdbe.org/4frw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4frw RCSB], [https://www.ebi.ac.uk/pdbsum/4frw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4frw ProSAT]</span></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=4frw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4frw OCA], [http://pdbe.org/4frw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4frw RCSB], [http://www.ebi.ac.uk/pdbsum/4frw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4frw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == 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> | + | [https://www.uniprot.org/uniprot/NECT4_HUMAN NECT4_HUMAN] Ectodermal dysplasia-pili torti-cutaneous syndactyly syndrome. The disease is caused by variants affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[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. | + | [https://www.uniprot.org/uniprot/NECT4_HUMAN NECT4_HUMAN] Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells. (Microbial infection) Acts as a receptor for measles virus.<ref>PMID:22048310</ref> <ref>PMID:23202587</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4frw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4frw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Poliovirus receptor-related protein|Poliovirus receptor-related protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Brasch, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Harrison, O J]] | + | [[Category: Brasch J]] |
| - | [[Category: Jin, X]] | + | [[Category: Harrison OJ]] |
| - | [[Category: Shapiro, L]] | + | [[Category: Jin X]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Shapiro L]] |
| - | [[Category: Ig domain]]
| + | |
| - | [[Category: Immunoglobulin-like domain]]
| + | |
| - | [[Category: Viral entry receptor]]
| + | |
| Structural highlights
Disease
NECT4_HUMAN Ectodermal dysplasia-pili torti-cutaneous syndactyly syndrome. The disease is caused by variants affecting the gene represented in this entry.
Function
NECT4_HUMAN Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells. (Microbial infection) Acts as a receptor for measles virus.[1] [2]
Publication Abstract from PubMed
Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues. Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning. We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern. To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5. All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer. However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction. The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
Nectin ectodomain structures reveal a canonical adhesive interface.,Harrison OJ, Vendome J, Brasch J, Jin X, Hong S, Katsamba PS, Ahlsen G, Troyanovsky RB, Troyanovsky SM, Honig B, Shapiro L Nat Struct Mol Biol. 2012 Aug 19. doi: 10.1038/nsmb.2366. PMID:22902367[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muhlebach MD, Mateo M, Sinn PL, Prufer S, Uhlig KM, Leonard VH, Navaratnarajah CK, Frenzke M, Wong XX, Sawatsky B, Ramachandran S, McCray PB Jr, Cichutek K, von Messling V, Lopez M, Cattaneo R. Adherens junction protein nectin-4 is the epithelial receptor for measles virus. Nature. 2011 Nov 2;480(7378):530-3. doi: 10.1038/nature10639. PMID:22048310 doi:http://dx.doi.org/10.1038/nature10639
- ↑ Zhang X, Lu G, Qi J, Li Y, He Y, Xu X, Shi J, Zhang CW, Yan J, Gao GF. Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4. Nat Struct Mol Biol. 2013 Jan;20(1):67-72. doi: 10.1038/nsmb.2432. Epub 2012 Dec , 2. PMID:23202587 doi:http://dx.doi.org/10.1038/nsmb.2432
- ↑ Harrison OJ, Vendome J, Brasch J, Jin X, Hong S, Katsamba PS, Ahlsen G, Troyanovsky RB, Troyanovsky SM, Honig B, Shapiro L. Nectin ectodomain structures reveal a canonical adhesive interface. Nat Struct Mol Biol. 2012 Aug 19. doi: 10.1038/nsmb.2366. PMID:22902367 doi:http://dx.doi.org/10.1038/nsmb.2366
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