6j2d: Difference between revisions
New page: '''Unreleased structure''' The entry 6j2d is ON HOLD Authors: Lu, D., Liu, K.F., Yue, C., Lu, Q., Cheng, H., Chai, Y., Qi, J.X., Gao, G.F., Liu, W.J. Description: Crystal structure of ... |
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==Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 in complex with Hendra virus-derived peptide HeV1== | |||
<StructureSection load='6j2d' size='340' side='right'caption='[[6j2d]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6j2d]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_hendraense Henipavirus hendraense] and [https://en.wikipedia.org/wiki/Pteropus_alecto Pteropus alecto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J2D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.313Å</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=6j2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j2d OCA], [https://pdbe.org/6j2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j2d RCSB], [https://www.ebi.ac.uk/pdbsum/6j2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j2d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A125R585_PTEAL A0A125R585_PTEAL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans. | |||
Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.,Lu D, Liu K, Zhang D, Yue C, Lu Q, Cheng H, Wang L, Chai Y, Qi J, Wang LF, Gao GF, Liu WJ PLoS Biol. 2019 Sep 9;17(9):e3000436. doi: 10.1371/journal.pbio.3000436., eCollection 2019 Sep. PMID:31498797<ref>PMID:31498797</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6j2d" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Gao | ==See Also== | ||
[[Category: | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
[[Category: | *[[MHC 3D structures|MHC 3D structures]] | ||
[[Category: | *[[MHC I 3D structures|MHC I 3D structures]] | ||
[[Category: Lu | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Henipavirus hendraense]] | |||
[[Category: Large Structures]] | |||
[[Category: Pteropus alecto]] | |||
[[Category: Chai Y]] | |||
[[Category: Cheng H]] | |||
[[Category: Gao GF]] | |||
[[Category: Liu KF]] | |||
[[Category: Liu WJ]] | |||
[[Category: Lu D]] | |||
[[Category: Lu Q]] | |||
[[Category: Qi JX]] | |||
[[Category: Yue C]] | |||
Latest revision as of 08:21, 21 November 2024
Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 in complex with Hendra virus-derived peptide HeV1Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 in complex with Hendra virus-derived peptide HeV1
Structural highlights
FunctionPublication Abstract from PubMedBats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans. Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.,Lu D, Liu K, Zhang D, Yue C, Lu Q, Cheng H, Wang L, Chai Y, Qi J, Wang LF, Gao GF, Liu WJ PLoS Biol. 2019 Sep 9;17(9):e3000436. doi: 10.1371/journal.pbio.3000436., eCollection 2019 Sep. PMID:31498797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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