5vx9

From Proteopedia

(Difference between revisions)

Revision as of 17:25, 11 December 2019

VP8* of P[6] Human Rotavirus RV3 in complex with LNFP1

Structural highlights

5vx9 is a 1 chain structure with sequence from Human group a rotavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[D7F7M7_9REOV] Outer capsid protein VP5*: Forms the spike "foot" and "body" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS01043052]

Publication Abstract from PubMed

Rotaviruses (RVs) cause life-threatening diarrhea in infants and children worldwide. Recent biochemical and epidemiological studies underscore the importance of histo-blood group antigens (HBGA) as both cell attachment and susceptibility factors for the globally dominant P[4], P[6], and P[8] genotypes of human RVs. How these genotypes interact with HBGA is not known. Here, our crystal structures of P[4] and a neonate-specific P[6] VP8*s alone and in complex with H-type I HBGA reveal a unique glycan binding site that is conserved in the globally dominant genotypes and allows for the binding of ABH HBGAs, consistent with their prevalence. Remarkably, the VP8* of P[6] RVs isolated from neonates displays subtle structural changes in this binding site that may restrict its ability to bind branched glycans. This provides a structural basis for the age-restricted tropism of some P[6] RVs as developmentally regulated unbranched glycans are more abundant in the neonatal gut.

Glycan recognition in globally dominant human rotaviruses.,Hu L, Sankaran B, Laucirica DR, Patil K, Salmen W, Ferreon ACM, Tsoi PS, Lasanajak Y, Smith DF, Ramani S, Atmar RL, Estes MK, Ferreon JC, Prasad BVV Nat Commun. 2018 Jul 6;9(1):2631. doi: 10.1038/s41467-018-05098-4. PMID:29980685^[1]

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

References

↑ Hu L, Sankaran B, Laucirica DR, Patil K, Salmen W, Ferreon ACM, Tsoi PS, Lasanajak Y, Smith DF, Ramani S, Atmar RL, Estes MK, Ferreon JC, Prasad BVV. Glycan recognition in globally dominant human rotaviruses. Nat Commun. 2018 Jul 6;9(1):2631. doi: 10.1038/s41467-018-05098-4. PMID:29980685 doi:http://dx.doi.org/10.1038/s41467-018-05098-4

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/5vx9"

@@ Line 1: / Line 1: @@
 ==VP8* of P[6] Human Rotavirus RV3 in complex with LNFP1==
-<StructureSection load='5vx9' size='340' side='right' caption='[[5vx9]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
+<StructureSection load='5vx9' size='340' side='right'caption='[[5vx9]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5vx9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VX9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5vx9]] is a 1 chain structure with sequence from [http://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=5VX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VX9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vx9 OCA], [http://pdbe.org/5vx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vx9 RCSB], [http://www.ebi.ac.uk/pdbsum/5vx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vx9 ProSAT]</span></td></tr>
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Human group a rotavirus]]
+[[Category: Large Structures]]
 [[Category: Hu, L]]
 [[Category: Prasad, B V.Venkataram]]

5vx9

From Proteopedia

Revision as of 17:25, 11 December 2019

VP8* of P[6] Human Rotavirus RV3 in complex with LNFP1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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