View source for 6ut9


==Crystal structure of the carbohydrate-binding domain VP8* of human P[4] rotavirus strain BM5265==
<StructureSection load='6ut9' size='340' side='right'caption='[[6ut9]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ut9]] is a 1 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=6UT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UT9 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]] 1.21&#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=6ut9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ut9 OCA], [https://pdbe.org/6ut9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ut9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ut9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ut9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E9BVI9_9VIRU E9BVI9_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Group A rotaviruses cause severe gastroenteritis in infants and young children worldwide, with P[II] genogroup rotaviruses (RVs) responsible for &gt;90% of global cases. RVs have diverse host ranges in different human and animal populations determined by host histo-blood group antigen (HBGA) receptor polymorphism, but details governing diversity, host ranges, and species barriers remain elusive. In this study, crystal structures of complexes of the major P[II] genogroup P[4] and P[8] genotype RV VP8* receptor-binding domains together with Lewis epitope-containing LNDFH I glycans in combination with VP8* receptor-glycan ligand affinity measurements based on NMR titration experiments revealed the structural basis for RV genotype-specific switching between betabeta and betaalpha HBGA receptor-binding sites that determine RV host ranges. The data support the hypothesis that P[II] RV evolution progressed from animals to humans under the selection of type 1 HBGAs guided by stepwise host synthesis of type 1 ABH and Lewis HBGAs. The results help explain disease burden, species barriers, epidemiology, and limited efficacy of current RV vaccines in developing countries. The structural data has the potential to impact the design of future vaccine strategies against RV gastroenteritis.

Structural basis of P[II] rotavirus evolution and host ranges under selection of histo-blood group antigens.,Xu S, McGinnis KR, Liu Y, Huang P, Tan M, Stuckert MR, Burnside RE, Jacob EG, Ni S, Jiang X, Kennedy MA Proc Natl Acad Sci U S A. 2021 Sep 7;118(36). pii: 2107963118. doi:, 10.1073/pnas.2107963118. PMID:34475219<ref>PMID:34475219</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ut9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human rotavirus A]]
[[Category: Large Structures]]
[[Category: Burnside R]]
[[Category: Jiang X]]
[[Category: Kennedy MA]]
[[Category: McGinnis K]]
[[Category: Stuckert M]]
[[Category: Xu S]]