6lnl

From Proteopedia

(Difference between revisions)

Current revision

ASFV core shell protein p15

Structural highlights

6lnl is a 3 chain structure with sequence from African swine fever virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9286Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PP62_ASFB7 Essential for the correct assembly and maturation of the core of the virion.^[1] Component of the core shell (PubMed:30185597). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (PubMed:32519301).^[2] ^[3] Component of the core shell (PubMed:30185597). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (PubMed:32451720).^[4] ^[5] Component of the core shell.^[6]

Publication Abstract from PubMed

African swine fever (ASF) is an acute, hemorrhagic, and highly contagious disease caused by African swine fever virus (ASFV). The mortality rate of acute infection up to 100% have posed an unprecedented challenge of the swine industry. Currently no commercial antiviral drug is available for the control and treatment of ASFV. The structural resolution of ASFV virions reveals the details of ASFV morphogenesis, providing a new perspective for the research and promotion of the development of ASFV vaccines. Although the architecture of ASFV have been solved via cryo-EM, the structural details of four of the five viral layers remain unclear (except the outer capsid). In this study, we resolved the crystal structure of the ASFV core shell protein p15. The secondary structural elements of a protomer include four alpha-helix structures and six antiparallel beta-strands. Further analysis revealed that ASFV p15 forms disulfide-linked trimers between the Cys9 from one protomer and Cys30 from other protomer. Additionally, the nucleic acid-binding property was characterized by electrophoretic mobility shift assay. Two critical amino acid Lys10 and Lys39 have been identified which is essential to the nucleic acid-binding affinity of ASFV p15. Together, these findings may provide new insight into antiviral drug development.

The structural basis of African swine fever virus core shell protein p15 binding to DNA.,Guo F, Shi Y, Yang M, Guo Y, Shen Z, Li M, Chen Y, Liang R, Yang Y, Chen H, Peng G FASEB J. 2021 Mar;35(3):e21350. doi: 10.1096/fj.202002145R. PMID:33629764^[7]

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

References

↑ Suarez C, Salas ML, Rodriguez JM. African swine fever virus polyprotein pp62 is essential for viral core development. J Virol. 2010 Jan;84(1):176-87. doi: 10.1128/JVI.01858-09. PMID:19846532 doi:http://dx.doi.org/10.1128/JVI.01858-09
↑ Alejo A, Matamoros T, Guerra M, Andres G. A Proteomic Atlas of the African Swine Fever Virus Particle. J Virol. 2018 Nov 12;92(23). pii: JVI.01293-18. doi: 10.1128/JVI.01293-18. Print , 2018 Dec 1. PMID:30185597 doi:http://dx.doi.org/10.1128/JVI.01293-18
↑ Li G, Fu D, Zhang G, Zhao D, Li M, Geng X, Sun D, Wang Y, Chen C, Jiao P, Cao L, Guo Y, Rao Z. Crystal structure of the African swine fever virus structural protein p35 reveals its role for core shell assembly. Protein Cell. 2020 Aug;11(8):600-605. doi: 10.1007/s13238-020-00730-w. PMID:32519301 doi:http://dx.doi.org/10.1007/s13238-020-00730-w
↑ Alejo A, Matamoros T, Guerra M, Andres G. A Proteomic Atlas of the African Swine Fever Virus Particle. J Virol. 2018 Nov 12;92(23). pii: JVI.01293-18. doi: 10.1128/JVI.01293-18. Print , 2018 Dec 1. PMID:30185597 doi:http://dx.doi.org/10.1128/JVI.01293-18
↑ Fu D, Zhao D, Zhang W, Zhang G, Li M, Zhang Z, Wang Y, Sun D, Jiao P, Chen C, Guo Y, Rao Z. Structure of African swine fever virus p15 reveals its dual role for membrane-association and DNA binding. Protein Cell. 2020 Aug;11(8):606-612. doi: 10.1007/s13238-020-00731-9. PMID:32451720 doi:http://dx.doi.org/10.1007/s13238-020-00731-9
↑ Alejo A, Matamoros T, Guerra M, Andres G. A Proteomic Atlas of the African Swine Fever Virus Particle. J Virol. 2018 Nov 12;92(23). pii: JVI.01293-18. doi: 10.1128/JVI.01293-18. Print , 2018 Dec 1. PMID:30185597 doi:http://dx.doi.org/10.1128/JVI.01293-18
↑ Guo F, Shi Y, Yang M, Guo Y, Shen Z, Li M, Chen Y, Liang R, Yang Y, Chen H, Peng G. The structural basis of African swine fever virus core shell protein p15 binding to DNA. FASEB J. 2021 Mar;35(3):e21350. doi: 10.1096/fj.202002145R. PMID:33629764 doi:http://dx.doi.org/10.1096/fj.202002145R

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6lnl"

Categories: African swine fever virus | Large Structures | Guo F | Peng G | Shi Y

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6lnl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/African_swine_fever_virus African swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LNL 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=6lnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnl OCA], [https://pdbe.org/6lnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnl RCSB], [https://www.ebi.ac.uk/pdbsum/6lnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnl ProSAT]</span></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]] 1.9286&#8491;</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=6lnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnl OCA], [https://pdbe.org/6lnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnl RCSB], [https://www.ebi.ac.uk/pdbsum/6lnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PP62_ASFB7 PP62_ASFB7]] Essential for the correct assembly and maturation of the core of the virion.<ref>PMID:19846532</ref>   Component of the core shell (PubMed:30185597). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (PubMed:32519301).<ref>PMID:30185597</ref> <ref>PMID:32519301</ref>   Component of the core shell (PubMed:30185597). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (PubMed:32451720).<ref>PMID:30185597</ref> <ref>PMID:32451720</ref>   Component of the core shell.<ref>PMID:30185597</ref>
+[https://www.uniprot.org/uniprot/PP62_ASFB7 PP62_ASFB7] Essential for the correct assembly and maturation of the core of the virion.<ref>PMID:19846532</ref>   Component of the core shell (PubMed:30185597). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (PubMed:32519301).<ref>PMID:30185597</ref> <ref>PMID:32519301</ref>   Component of the core shell (PubMed:30185597). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (PubMed:32451720).<ref>PMID:30185597</ref> <ref>PMID:32451720</ref>   Component of the core shell.<ref>PMID:30185597</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

6lnl

From Proteopedia

Current revision

ASFV core shell protein p15

Structural highlights

Function

Publication Abstract from PubMed

References

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