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==AALALL segment from the Nucleoprotein of SARS-CoV-2, residues 217-222, crystal form 2==
==AALALL segment from the Nucleoprotein of SARS-CoV-2, residues 217-222, crystal form 2==
<StructureSection load='7lux' size='340' side='right'caption='[[7lux]]' scene=''>
<StructureSection load='7lux' size='340' side='right'caption='[[7lux]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUX FirstGlance]. <br>
<table><tr><td colspan='2'>[[7lux]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUX FirstGlance]. <br>
</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=7lux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lux OCA], [https://pdbe.org/7lux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lux RCSB], [https://www.ebi.ac.uk/pdbsum/7lux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lux ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7ltu|7ltu]]</div></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=7lux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lux OCA], [https://pdbe.org/7lux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lux RCSB], [https://www.ebi.ac.uk/pdbsum/7lux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lux ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/NCAP_SARS2 NCAP_SARS2]] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The SARS-CoV-2 Nucleoprotein (NCAP) functions in RNA packaging during viral replication and assembly. Computational analysis of its amino acid sequence reveals a central low-complexity domain (LCD) having sequence features akin to LCDs in other proteins known to function in liquid-liquid phase separation. Here we show that in the presence of viral RNA, NCAP, and also its LCD segment alone, form amyloid-like fibrils when undergoing liquid-liquid phase separation. Within the LCD we identified three 6-residue segments that drive amyloid fibril formation. We determined atomic structures for fibrils formed by each of the three identified segments. These structures informed our design of peptide inhibitors of NCAP fibril formation and liquid-liquid phase separation, suggesting a therapeutic route for Covid-19. One Sentence Summary: Atomic structures of amyloid-driving peptide segments from SARS-CoV-2 Nucleoprotein inform the development of Covid-19 therapeutics.
Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2.,Tayeb-Fligelman E, Cheng X, Tai C, Bowler JT, Griner S, Sawaya MR, Seidler PM, Jiang YX, Lu J, Rosenberg GM, Salwinski L, Abskharon R, Zee CT, Hou K, Li Y, Boyer DR, Murray KA, Falcon G, Anderson DH, Cascio D, Saelices L, Damoiseaux R, Guo F, Eisenberg DS bioRxiv. 2021 Mar 5. doi: 10.1101/2021.03.05.434000. PMID:33688654<ref>PMID:33688654</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lux" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eisenberg DS]]
[[Category: Eisenberg, D S]]
[[Category: Lu J]]
[[Category: Lu, J]]
[[Category: Rodriguez JA]]
[[Category: Rodriguez, J A]]
[[Category: Sawaya MR]]
[[Category: Sawaya, M R]]
[[Category: Zee C-T]]
[[Category: Zee, C T]]
[[Category: Amyloid fibril]]
[[Category: Protein fibril]]

Revision as of 09:55, 24 March 2021

AALALL segment from the Nucleoprotein of SARS-CoV-2, residues 217-222, crystal form 2AALALL segment from the Nucleoprotein of SARS-CoV-2, residues 217-222, crystal form 2

Structural highlights

7lux is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NCAP_SARS2] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.

Publication Abstract from PubMed

The SARS-CoV-2 Nucleoprotein (NCAP) functions in RNA packaging during viral replication and assembly. Computational analysis of its amino acid sequence reveals a central low-complexity domain (LCD) having sequence features akin to LCDs in other proteins known to function in liquid-liquid phase separation. Here we show that in the presence of viral RNA, NCAP, and also its LCD segment alone, form amyloid-like fibrils when undergoing liquid-liquid phase separation. Within the LCD we identified three 6-residue segments that drive amyloid fibril formation. We determined atomic structures for fibrils formed by each of the three identified segments. These structures informed our design of peptide inhibitors of NCAP fibril formation and liquid-liquid phase separation, suggesting a therapeutic route for Covid-19. One Sentence Summary: Atomic structures of amyloid-driving peptide segments from SARS-CoV-2 Nucleoprotein inform the development of Covid-19 therapeutics.

Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2.,Tayeb-Fligelman E, Cheng X, Tai C, Bowler JT, Griner S, Sawaya MR, Seidler PM, Jiang YX, Lu J, Rosenberg GM, Salwinski L, Abskharon R, Zee CT, Hou K, Li Y, Boyer DR, Murray KA, Falcon G, Anderson DH, Cascio D, Saelices L, Damoiseaux R, Guo F, Eisenberg DS bioRxiv. 2021 Mar 5. doi: 10.1101/2021.03.05.434000. PMID:33688654[1]

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

References

  1. Tayeb-Fligelman E, Cheng X, Tai C, Bowler JT, Griner S, Sawaya MR, Seidler PM, Jiang YX, Lu J, Rosenberg GM, Salwinski L, Abskharon R, Zee CT, Hou K, Li Y, Boyer DR, Murray KA, Falcon G, Anderson DH, Cascio D, Saelices L, Damoiseaux R, Guo F, Eisenberg DS. Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 2021 Mar 5. doi: 10.1101/2021.03.05.434000. PMID:33688654 doi:http://dx.doi.org/10.1101/2021.03.05.434000

7lux, resolution 1.30Å

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