2vis: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='2vis' size='340' side='right'caption='[[2vis]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
<StructureSection load='2vis' size='340' side='right'caption='[[2vis]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vis]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/I000x I000x] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VIS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vis]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/X-31(H3N2)) Influenza A virus (A/X-31(H3N2))] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.25&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vis OCA], [http://pdbe.org/2vis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vis RCSB], [http://www.ebi.ac.uk/pdbsum/2vis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vis ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2vis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vis OCA], [https://pdbe.org/2vis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vis RCSB], [https://www.ebi.ac.uk/pdbsum/2vis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vis ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
[https://www.uniprot.org/uniprot/Q99LC4_MOUSE Q99LC4_MOUSE]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 14: Line 15:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vis_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vis_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
Line 35: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: I000x]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Bizebard, T]]
[[Category: Bizebard T]]
[[Category: Fleury, D]]
[[Category: Fleury D]]
[[Category: Gigant, B]]
[[Category: Gigant B]]
[[Category: Knossow, M]]
[[Category: Knossow M]]
[[Category: Skehel, J J]]
[[Category: Skehel JJ]]
[[Category: Wharton, S A]]
[[Category: Wharton SA]]
[[Category: Glycoprotein]]

Latest revision as of 11:40, 30 October 2024

INFLUENZA VIRUS HEMAGGLUTININ, (ESCAPE) MUTANT WITH THR 131 REPLACED BY ILE, COMPLEXED WITH A NEUTRALIZING ANTIBODYINFLUENZA VIRUS HEMAGGLUTININ, (ESCAPE) MUTANT WITH THR 131 REPLACED BY ILE, COMPLEXED WITH A NEUTRALIZING ANTIBODY

Structural highlights

2vis is a 3 chain structure with sequence from Influenza A virus (A/X-31(H3N2)) and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.25Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q99LC4_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the hemagglutinin (HA) of a mutant influenza virus that escapes neutralization by a monoclonal antibody shows that the mutation causes changes in HA structure which avoid an energetically less favorable conformation. However, the structure of the mutant HA.Fab complex indicates that the antibody binds selectively to mutant HA in a wild type-like distorted conformation. The association of an antibody with a less favored HA conformation represents an alternative to previously described mechanisms of escape from neutralization by antibodies.

Antigen distortion allows influenza virus to escape neutralization.,Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T Nat Struct Biol. 1998 Feb;5(2):119-23. PMID:9461077[1]

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

See Also

References

  1. ↑ Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T. Antigen distortion allows influenza virus to escape neutralization. Nat Struct Biol. 1998 Feb;5(2):119-23. PMID:9461077

2vis, resolution 3.25Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2vis&oldid=4197473"