4hlz

From Proteopedia

(Difference between revisions)

Revision as of 08:25, 3 November 2022

Crystal Structure of Fab C179 in Complex with a H2N2 influenza virus hemagglutinin

Structural highlights

4hlz is a 12 chain structure with sequence from Influenza A virus (A/Japan/305/1957(H2N2)) and Mus musculus. 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

C7S226_I57A0 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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643]

Publication Abstract from PubMed

We report structural characterization of the first antibody identified to cross-neutralize multiple subtypes of influenza A viruses. The crystal structure of mouse antibody C179 bound to the pandemic 1957 H2N2 hemagglutinin (HA) reveals that it targets a similar epitope on the HA stem as the recently identified human broadly neutralizing antibodies (bnAbs). C179 also inhibits the low-pH conformational change of the HA, but uses a different angle of approach and both heavy and light chains.

Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 hemagglutinin.,Dreyfus C, Ekiert DC, Wilson IA J Virol. 2013 Apr 3. PMID:23552413^[1]

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

References

↑ Dreyfus C, Ekiert DC, Wilson IA. Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 hemagglutinin. J Virol. 2013 Apr 3. PMID:23552413 doi:10.1128/JVI.02975-12

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4hlz"

Categories: Large Structures | Mus musculus | Dreyfus C | Wilson IA

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Fab C179 in Complex with a H2N2 influenza virus hemagglutinin==
-<StructureSection load='4hlz' size='340' side='right' caption='[[4hlz]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='4hlz' size='340' side='right'caption='[[4hlz]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4hlz]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/I57a0 I57a0] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HLZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4hlz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Japan/305/1957(H2N2)) Influenza A virus (A/Japan/305/1957(H2N2))] 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=4HLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HLZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=387161 I57A0])</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=4hlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hlz OCA], [https://pdbe.org/4hlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hlz RCSB], [https://www.ebi.ac.uk/pdbsum/4hlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hlz ProSAT]</span></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=4hlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hlz OCA], [http://pdbe.org/4hlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hlz RCSB], [http://www.ebi.ac.uk/pdbsum/4hlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hlz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C7S226_I57A0 C7S226_I57A0]] 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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643]
+[https://www.uniprot.org/uniprot/C7S226_I57A0 C7S226_I57A0] 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 (By similarity).[RuleBase:RU003324][SAAS:SAAS013829_004_327643]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: I57a0]]
+[[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Dreyfus, C]]
+[[Category: Dreyfus C]]
-[[Category: Wilson, I A]]
+[[Category: Wilson IA]]
-[[Category: Antibody affinity]]
-[[Category: Antigen]]
-[[Category: Avian flu]]
-[[Category: Envelope protein]]
-[[Category: Epitope]]
-[[Category: Glycosylation]]
-[[Category: H2n2 subtype]]
-[[Category: Hemagglutinin glycoprotein]]
-[[Category: Immunoglobulin fab fragment]]
-[[Category: Influenza vaccine]]
-[[Category: Neutralizing antibody]]
-[[Category: Viral protein-immune system complex]]

4hlz

From Proteopedia

Revision as of 08:25, 3 November 2022

Crystal Structure of Fab C179 in Complex with a H2N2 influenza virus hemagglutinin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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