8d21: Difference between revisions

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'''Unreleased structure'''


The entry 8d21 is ON HOLD  until Paper Publication
==Cryo-EM structure of the VRC321 clinical trial, vaccine-elicited, human antibody 1B06 in complex with a stabilized NC99 HA trimer==
 
<StructureSection load='8d21' size='340' side='right'caption='[[8d21]], [[Resolution|resolution]] 3.96&Aring;' scene=''>
Authors: Gorman, J., Kwong, P.D.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8d21]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D21 FirstGlance]. <br>
Description: Cryo-EM structure of the VRC321 clinical trial, vaccine-elicited, human antibody 1B06 in complex with a stabilized NC99 HA trimer
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d21 OCA], [https://pdbe.org/8d21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d21 RCSB], [https://www.ebi.ac.uk/pdbsum/8d21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d21 ProSAT]</span></td></tr>
[[Category: Gorman, J]]
</table>
[[Category: Kwong, P.D]]
== Function ==
[https://www.uniprot.org/uniprot/HEMA_I00A1 HEMA_I00A1] 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 either through clathrin-dependent endocytosis or through 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.[HAMAP-Rule:MF_04072]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Influenza A virus]]
[[Category: Large Structures]]
[[Category: Gorman J]]
[[Category: Kwong PD]]

Revision as of 23:30, 12 April 2023

Cryo-EM structure of the VRC321 clinical trial, vaccine-elicited, human antibody 1B06 in complex with a stabilized NC99 HA trimerCryo-EM structure of the VRC321 clinical trial, vaccine-elicited, human antibody 1B06 in complex with a stabilized NC99 HA trimer

Structural highlights

8d21 is a 12 chain structure with sequence from Homo sapiens and Influenza A virus. 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

HEMA_I00A1 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 either through clathrin-dependent endocytosis or through 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.[HAMAP-Rule:MF_04072]

8d21, resolution 3.96Å

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OCA