4gjt

From Proteopedia

(Difference between revisions)

Current revision

complex structure of nectin-4 bound to MV-H

Structural highlights

4gjt is a 3 chain structure with sequence from Homo sapiens and Measles virus strain Ichinose-B95a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1001Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gjt"

@@ Line 1: / Line 1: @@
 ==complex structure of nectin-4 bound to MV-H==
-<StructureSection load='4gjt' size='340' side='right' caption='[[4gjt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='4gjt' size='340' side='right'caption='[[4gjt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4gjt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Measc Measc]. 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>
+<table><tr><td colspan='2'>[[4gjt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4GJT FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1001&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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 MEASC]), LNIR, nectin-4, PRR4, PVRL4 ([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=4gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gjt OCA], [https://pdbe.org/4gjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gjt RCSB], [https://www.ebi.ac.uk/pdbsum/4gjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gjt 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=4gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gjt OCA], [http://pdbe.org/4gjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gjt RCSB], [http://www.ebi.ac.uk/pdbsum/4gjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gjt ProSAT]</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>
 == 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.
+[https://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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 19: @@
 </div>
 <div class="pdbe-citations 4gjt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Poliovirus receptor-related protein|Poliovirus receptor-related protein]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Measc]]
+[[Category: Large Structures]]
-[[Category: Gao, G F]]
+[[Category: Measles virus strain Ichinose-B95a]]
-[[Category: He, Y]]
+[[Category: Gao GF]]
-[[Category: Li, Y]]
+[[Category: He Y]]
-[[Category: Lu, G]]
+[[Category: Li Y]]
-[[Category: Qi, J]]
+[[Category: Lu G]]
-[[Category: Shi, J]]
+[[Category: Qi J]]
-[[Category: Xu, X]]
+[[Category: Shi J]]
-[[Category: Yan, J]]
+[[Category: Xu X]]
-[[Category: Zhang, C]]
+[[Category: Yan J]]
-[[Category: Zhang, X]]
+[[Category: Zhang C]]
-[[Category: Beta4/beta5 groove]]
+[[Category: Zhang X]]
-[[Category: Igv-like fold]]
-[[Category: Membrane protein-viral protein complex]]
-[[Category: Mv-h]]
-[[Category: Nectin-4]]
-[[Category: Six-bladed -propeller]]
-[[Category: Viral entry]]

4gjt

From Proteopedia

Current revision

complex structure of nectin-4 bound to MV-H

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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