7ki5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of P[6] rotavirus vp8* in complex with LNT==
==Crystal structure of P[6] rotavirus vp8* in complex with LNT==
-
<StructureSection load='7ki5' size='340' side='right'caption='[[7ki5]]' scene=''>
+
<StructureSection load='7ki5' size='340' side='right'caption='[[7ki5]], [[Resolution|resolution]] 1.52&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=7KI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KI5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7ki5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_group_a_rotavirus Human group a rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KI5 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=7ki5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ki5 OCA], [https://pdbe.org/7ki5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ki5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ki5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ki5 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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10941 Human group A rotavirus])</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=7ki5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ki5 OCA], [https://pdbe.org/7ki5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ki5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ki5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ki5 ProSAT]</span></td></tr>
</table>
</table>
 +
<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 7ki5" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Human group a rotavirus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Kennedy MA]]
+
[[Category: Kennedy, M A]]
-
[[Category: Xu S]]
+
[[Category: Xu, S]]
 +
[[Category: Host receptor interaction]]
 +
[[Category: Rotavirus]]
 +
[[Category: Viral protein]]
 +
[[Category: Virus]]

Revision as of 07:00, 22 September 2021

Crystal structure of P[6] rotavirus vp8* in complex with LNT

PDB ID 7ki5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools