3hag

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:58, 21 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3hag' size='340' side='right'caption='[[3hag]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='3hag' size='340' side='right'caption='[[3hag]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3hag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hev Hev]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3hag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orthohepevirus_A Orthohepevirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAG 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=3hag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hag OCA], [https://pdbe.org/3hag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hag RCSB], [https://www.ebi.ac.uk/pdbsum/3hag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hag ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#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=3hag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hag OCA], [https://pdbe.org/3hag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hag RCSB], [https://www.ebi.ac.uk/pdbsum/3hag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hag ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/CAPSD_HEVCT CAPSD_HEVCT] Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.[UniProtKB:Q9YLQ9] Forms an icosahedral capsid with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60 copies linked to each other. Binds to the 5' end of the genomic RNA to mediate genome encapsidation (By similarity). Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry. Additionally, the interactions with host ASGR1 and ASGR2 facilitate viral infection of hepatocytes (By similarity). Inhibits IFN production by blocking host TBK1-induced IRF3 phosphorylation (By similarity). The nuclear form probably modulates host gene expression (By similarity).[UniProtKB:P29326][UniProtKB:P33426][UniProtKB:Q81871]
-
Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-A structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.
+
-
 
+
-
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.,Guu TS, Liu Z, Ye Q, Mata DA, Li K, Yin C, Zhang J, Tao YJ Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):12992-7. Epub 2009 Jul 21. PMID:19622744<ref>PMID:19622744</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3hag" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Hev]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Guu, T S.Y]]
+
[[Category: Orthohepevirus A]]
-
[[Category: Li, K]]
+
[[Category: Guu TSY]]
-
[[Category: Liu, Z]]
+
[[Category: Li K]]
-
[[Category: Mata, D A]]
+
[[Category: Liu Z]]
-
[[Category: Tao, Y J]]
+
[[Category: Mata DA]]
-
[[Category: Ye, Q]]
+
[[Category: Tao YJ]]
-
[[Category: Yin, C]]
+
[[Category: Ye Q]]
-
[[Category: Zhang, J]]
+
[[Category: Yin C]]
-
[[Category: Beta barrel]]
+
[[Category: Zhang J]]
-
[[Category: Icosahedral virus]]
+
-
[[Category: Jelly-roll beta sheet]]
+
-
[[Category: Virus]]
+

Current revision

Crystal structure of the Hepatitis E Virus-like Particle

PDB ID 3hag

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hag"
Personal tools