6oai: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
m Protected "6oai" [edit=sysop:move=sysop]
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 6oai is ON HOLD
==Crystal structure of P[6] rotavirus vp8* complexed with LNFPI==
<StructureSection load='6oai' size='340' side='right'caption='[[6oai]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oai]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_rotavirus_A Human rotavirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAI 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6oai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oai OCA], [https://pdbe.org/6oai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oai RCSB], [https://www.ebi.ac.uk/pdbsum/6oai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oai ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D2DXN5_9VIRU D2DXN5_9VIRU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Initial cell attachment of rotavirus (RV) to specific cell surface glycan receptors, which is the essential first step in RV infection, is mediated by the VP8* domain of the spike protein VP4. Recently, human histo-blood group antigens (HBGAs) have been identified as receptors or attachment factors for human RV strains. RV strains in the P[4] and P[8] genotypes of the P[II] genogroup share common recognition of the Lewis b (Leb) and H type 1 antigens, however, the molecular basis of receptor recognition by the major human P[8] RVs remains unknown due to lack of experimental structural information. Here, we used nuclear magnetic resonance (NMR) spectroscopy-based titration experiments and NMR-derived high ambiguity driven docking (HADDOCK) methods to elucidate the molecular basis for P[8] VP8* recognition of the Leb (LNDFH I) and type 1 HBGAs. We also used X-ray crystallography to determine the molecular details underlying P[6] recognition of H type 1 HBGAs. Unlike P[6]/P[19] VP8*s that recognize H type 1 HBGAs in a binding surface composed of an alpha-helix and a beta-sheet, referred as the "betaalpha binding site", the P[8] and P[4] VP8*s bind Leb HBGAs in a previously undescribed pocket formed by the edges of two beta-sheets, referred to as the "betabeta binding site". Importantly, the P[8] and P[4] VP8*s retain binding capability to non-Leb type 1 HBGAs using the betaalpha binding site. The presence of two distinct binding sites for Leb and non-Leb HBGA glycans in the P[8] and P[4] VP8* domains suggests host-pathogen co-evolution under structural and functional adaptation of RV pathogens to host glycan polymorphisms. Assessment and understanding of the precise impact of this co-evolutionary process in determining RV host ranges and cross-species RV transmission should facilitate improved RV vaccine development and prediction of future RV strain emergence and epidemics.


Authors: Xu, S., Liu, Y., Jiang, X., Kennedy, M.A.
Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens.,Xu S, Ahmed LU, Stuckert MR, McGinnis KR, Liu Y, Tan M, Huang P, Zhong W, Zhao D, Jiang X, Kennedy MA PLoS Pathog. 2020 Mar 24;16(3):e1008386. doi: 10.1371/journal.ppat.1008386., eCollection 2020 Mar. PMID:32208455<ref>PMID:32208455</ref>


Description: Crystal structure of P[6] rotavirus vp8* complexed with LNFPI
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Xu, S]]
<div class="pdbe-citations 6oai" style="background-color:#fffaf0;"></div>
[[Category: Kennedy, M.A]]
== References ==
[[Category: Liu, Y]]
<references/>
[[Category: Jiang, X]]
__TOC__
</StructureSection>
[[Category: Human rotavirus A]]
[[Category: Large Structures]]
[[Category: Jiang X]]
[[Category: Kennedy MA]]
[[Category: Liu Y]]
[[Category: Xu S]]
Retrieved from "https://proteopedia.org/6oai"