This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4rox

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:54, 1 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='4rox' size='340' side='right'caption='[[4rox]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='4rox' size='340' side='right'caption='[[4rox]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4rox]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Norovirus_hu/gii.1/7ek/hawaii/1971/usa Norovirus hu/gii.1/7ek/hawaii/1971/usa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ROX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ROX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4rox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/GII.1/7EK/Hawaii/1971/USA Norovirus Hu/GII.1/7EK/Hawaii/1971/USA]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ROX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ROX FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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]] 1.89&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP1, U07611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1208060 Norovirus Hu/GII.1/7EK/Hawaii/1971/USA])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rox OCA], [http://pdbe.org/4rox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rox RCSB], [http://www.ebi.ac.uk/pdbsum/4rox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rox ProSAT]</span></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=4rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rox OCA], [https://pdbe.org/4rox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rox RCSB], [https://www.ebi.ac.uk/pdbsum/4rox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rox ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/J9XXB7_9CALI J9XXB7_9CALI]
-
Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.
+
-
Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens.,Singh BK, Leuthold MM, Hansman GS mSphere. 2016 Mar 30;1(2). pii: e00049-16. doi: 10.1128/mSphere.00049-16., eCollection 2016 Mar-Apr. PMID:27303720<ref>PMID:27303720</ref>
+
==See Also==
-
 
+
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4rox" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Norovirus hu/gii 1/7ek/hawaii/1971/usa]]
+
[[Category: Norovirus Hu/GII 1/7EK/Hawaii/1971/USA]]
-
[[Category: Hansman, G S]]
+
[[Category: Hansman GS]]
-
[[Category: Singh, B K]]
+
[[Category: Singh BK]]
-
[[Category: Hbga]]
+
-
[[Category: Protruding domain]]
+
-
[[Category: Surface domain]]
+
-
[[Category: Viral protein]]
+
-
[[Category: Virus binding]]
+
-
[[Category: Virus surface]]
+

Current revision

Crystal Structure of P Domain of Hawaii Norovirus (GII.1)

PDB ID 4rox

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/4rox"
Personal tools