1aol
From Proteopedia
(Difference between revisions)
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<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOL FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [https://pdbe.org/1aol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [https://www.ebi.ac.uk/pdbsum/1aol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol ProSAT]</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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [https://pdbe.org/1aol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [https://www.ebi.ac.uk/pdbsum/1aol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aol ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aol ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus. | ||
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| - | Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.,Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219<ref>PMID:9287219</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1aol" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Friend murine leukemia virus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berger | + | [[Category: Berger JM]] |
| - | [[Category: Cunningham | + | [[Category: Cunningham JM]] |
| - | [[Category: Davey | + | [[Category: Davey RA]] |
| - | [[Category: Fass | + | [[Category: Fass D]] |
| - | [[Category: Hamson | + | [[Category: Hamson CA]] |
| - | [[Category: Kim | + | [[Category: Kim PS]] |
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Revision as of 15:26, 13 March 2024
FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN
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