5oyl

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==VSV G CR2==
==VSV G CR2==
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<StructureSection load='5oyl' size='340' side='right' caption='[[5oyl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='5oyl' size='340' side='right'caption='[[5oyl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5oyl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Recombinant_vesicular_stomatitis_indiana_virus_rvsv-g/gfp Recombinant vesicular stomatitis indiana virus rvsv-g/gfp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OYL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5oyl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Recombinant_vesicular_stomatitis_Indiana_virus_rVSV-G/GFP Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OYL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5oy9|5oy9]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyl OCA], [https://pdbe.org/5oyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oyl RCSB], [https://www.ebi.ac.uk/pdbsum/5oyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyl ProSAT]</span></td></tr>
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<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=5oyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyl OCA], [http://pdbe.org/5oyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oyl RCSB], [http://www.ebi.ac.uk/pdbsum/5oyl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyl ProSAT]</span></td></tr>
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</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/LDLR_HUMAN LDLR_HUMAN]] Defects in LDLR are the cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]; a common autosomal semi-dominant disease that affects about 1 in 500 individuals. The receptor defect impairs the catabolism of LDL, and the resultant elevation in plasma LDL-cholesterol promotes deposition of cholesterol in the skin (xanthelasma), tendons (xanthomas), and coronary arteries (atherosclerosis).<ref>PMID:3263645</ref> <ref>PMID:2569482</ref> <ref>PMID:3955657</ref> <ref>PMID:8347689</ref> <ref>PMID:2318961</ref> <ref>PMID:1446662</ref> <ref>PMID:1867200</ref> <ref>PMID:8462973</ref> <ref>PMID:8168830</ref> <ref>PMID:2726768</ref> <ref>PMID:1464748</ref> <ref>PMID:7573037</ref> <ref>PMID:7583548</ref> <ref>PMID:7550239</ref> <ref>PMID:7635461</ref> <ref>PMID:7635482</ref> <ref>PMID:7649546</ref> <ref>PMID:7649549</ref> <ref>PMID:8740918</ref> <ref>PMID:8664907</ref> <ref>PMID:9026534</ref> <ref>PMID:9254862</ref> <ref>PMID:9143924</ref> <ref>PMID:9259195</ref> <ref>PMID:9104431</ref> <ref>PMID:9654205</ref> <ref>PMID:9452094</ref> <ref>PMID:9452095</ref> <ref>PMID:9452118</ref> <ref>PMID:10206683</ref> <ref>PMID:10660340</ref> [:]<ref>PMID:9852677</ref> <ref>PMID:9678702</ref> <ref>PMID:10422803</ref> <ref>PMID:10090484</ref> <ref>PMID:10447263</ref> <ref>PMID:10978268</ref> <ref>PMID:10980548</ref> <ref>PMID:10882754</ref> <ref>PMID:11298688</ref> <ref>PMID:17142622</ref> <ref>PMID:19319977</ref> <ref>PMID:22160468</ref>
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LDLR_HUMAN LDLR_HUMAN]] Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. In case of HIV-1 infection, functions as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells.
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[https://www.uniprot.org/uniprot/B7UCZ5_9RHAB B7UCZ5_9RHAB]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vesicular stomatitis virus (VSV) is an oncolytic rhabdovirus and its glycoprotein G is widely used to pseudotype other viruses for gene therapy. Low-density lipoprotein receptor (LDL-R) serves as a major entry receptor for VSV. Here we report two crystal structures of VSV G in complex with two distinct cysteine-rich domains (CR2 and CR3) of LDL-R, showing that their binding sites on G are identical. We identify two basic residues on G, which are essential for its interaction with CR2 and CR3. Mutating these residues abolishes VSV infectivity even though VSV can use alternative receptors, indicating that all VSV receptors are members of the LDL-R family. Collectively, our data suggest that VSV G has specifically evolved to interact with receptor CR domains. These structural insights into the interaction between VSV G and host cell receptors provide a basis for the design of recombinant viruses with an altered tropism.
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Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein.,Nikolic J, Belot L, Raux H, Legrand P, Gaudin Y, A Albertini A Nat Commun. 2018 Mar 12;9(1):1029. doi: 10.1038/s41467-018-03432-4. PMID:29531262<ref>PMID:29531262</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5oyl" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[LDL receptor|LDL receptor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Recombinant vesicular stomatitis indiana virus rvsv-g/gfp]]
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[[Category: Homo sapiens]]
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[[Category: Albertini, A A]]
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[[Category: Large Structures]]
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[[Category: Belot, L]]
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[[Category: Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP]]
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[[Category: Gaudin, Y]]
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[[Category: Albertini AA]]
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[[Category: Legrand, P]]
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[[Category: Belot L]]
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[[Category: Viral protein]]
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[[Category: Gaudin Y]]
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[[Category: Legrand P]]

Current revision

VSV G CR2

PDB ID 5oyl

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