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1ha0

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(New page: 200px<br /><applet load="1ha0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ha0, resolution 2.80&Aring;" /> '''HEMAGGLUTININ PRECUR...)
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[[Image:1ha0.gif|left|200px]]<br /><applet load="1ha0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ha0, resolution 2.80&Aring;" />
 
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'''HEMAGGLUTININ PRECURSOR HA0'''<br />
 
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==Overview==
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==HEMAGGLUTININ PRECURSOR HA0==
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The membrane fusion potential of influenza HA, like many viral, membrane-fusion glycoproteins, is generated by proteolytic cleavage of a, biosynthetic precursor. The three-dimensional structure of ectodomain of, the precursor HA0 has been determined and compared with that of cleaved, HA. The cleavage site is a prominent surface loop adjacent to a novel, cavity; cleavage results in structural rearrangements in which the, nonpolar amino acids near the new amino terminus bury ionizable residues, in the cavity that are implicated in the low-pH-induced conformational, change. Amino acid insertions at the cleavage site in HAs of virulent, avian viruses and those of viruses isolated from the recent severe, outbreak of influenza in humans in Hong Kong would extend this surface, loop, facilitating intracellular cleavage.
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<StructureSection load='1ha0' size='340' side='right'caption='[[1ha0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ha0]] is a 1 chain structure with sequence from [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=1HA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HA0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ha0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ha0 OCA], [https://pdbe.org/1ha0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ha0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ha0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ha0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/1ha0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ha0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HA0 OCA].
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation., Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC, Cell. 1998 Oct 30;95(3):409-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9814710 9814710]
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[[Category: Influenza A virus]]
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[[Category: Influenza a virus]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen J]]
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[[Category: Chen, J.]]
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[[Category: Ho Lee K]]
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[[Category: Lee, K.Ho.]]
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[[Category: Skehel JJ]]
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[[Category: Skehel, J.J.]]
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[[Category: Steinhauer DA]]
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[[Category: Steinhauer, D.A.]]
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[[Category: Stevens DJ]]
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[[Category: Stevens, D.J.]]
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[[Category: Wiley DC]]
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[[Category: Wiley, D.C.]]
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[[Category: NAG]]
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[[Category: glycoprotein]]
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[[Category: membrane-fusion precursor]]
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[[Category: virus/viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:28:36 2007''
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Current revision

HEMAGGLUTININ PRECURSOR HA0

PDB ID 1ha0

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