4jpr: Difference between revisions

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==Structure of the ASLV fusion subunit core==
==Structure of the ASLV fusion subunit core==
<StructureSection load='4jpr' size='340' side='right' caption='[[4jpr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4jpr' size='340' side='right'caption='[[4jpr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jpr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Avian_leukosis_virus_rsa Avian leukosis virus rsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JPR FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jpr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus_(strain_Schmidt-Ruppin_A) Rous sarcoma virus (strain Schmidt-Ruppin A)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JPR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jf3|4jf3]], [[4jgs|4jgs]]</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=4jpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpr OCA], [https://pdbe.org/4jpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpr RCSB], [https://www.ebi.ac.uk/pdbsum/4jpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpr ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">env ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269446 Avian leukosis virus RSA])</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=4jpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpr OCA], [http://pdbe.org/4jpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jpr RCSB], [http://www.ebi.ac.uk/pdbsum/4jpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ENV_RSVSA ENV_RSVSA]] 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).  
[https://www.uniprot.org/uniprot/ENV_RSVSA ENV_RSVSA] 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).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Avian leukosis virus rsa]]
[[Category: Large Structures]]
[[Category: Aydin, H]]
[[Category: Aydin H]]
[[Category: Lee, J E]]
[[Category: Lee JE]]
[[Category: Smrke, B M]]
[[Category: Smrke BM]]
[[Category: Alpha-helix six-helix bundle]]
[[Category: Membrane fusion]]
[[Category: Viral protein]]

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