1htm

From Proteopedia

(Difference between revisions)

Current revision

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

Structural highlights

1htm is a 6 chain structure with sequence from Uncultured beta proteobacterium UMTRA-608. The April 2006 RCSB PDB Molecule of the Month feature on Hemagglutinin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Publication Abstract from PubMed

Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 A to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.

Structure of influenza haemagglutinin at the pH of membrane fusion.,Bullough PA, Hughson FM, Skehel JJ, Wiley DC Nature. 1994 Sep 1;371(6492):37-43. PMID:8072525^[1]

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

References

↑ Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 1994 Sep 1;371(6492):37-43. PMID:8072525 doi:http://dx.doi.org/10.1038/371037a0

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/1htm"

@@ Line 3: / Line 3: @@
 <StructureSection load='1htm' size='340' side='right'caption='[[1htm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1htm]] is a 6 chain structure. The April 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hemagglutinin''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_4 10.2210/rcsb_pdb/mom_2006_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1htm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_beta_proteobacterium_UMTRA-608 Uncultured beta proteobacterium UMTRA-608]. The April 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hemagglutinin''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_4 10.2210/rcsb_pdb/mom_2006_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTM 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=1htm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htm OCA], [https://pdbe.org/1htm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htm RCSB], [https://www.ebi.ac.uk/pdbsum/1htm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htm 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]] 2.5&#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=1htm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htm OCA], [https://pdbe.org/1htm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htm RCSB], [https://www.ebi.ac.uk/pdbsum/1htm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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/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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 28: @@
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Bullough, P A]]
+[[Category: Uncultured beta proteobacterium UMTRA-608]]
-[[Category: Hughson, F M]]
+[[Category: Bullough PA]]
-[[Category: Skehel, J J]]
+[[Category: Hughson FM]]
-[[Category: Wiley, D C]]
+[[Category: Skehel JJ]]
-[[Category: Influenza virus hemagglutinin]]
+[[Category: Wiley DC]]
-[[Category: Viral protein]]

1htm

From Proteopedia

Current revision

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox