2rft: Difference between revisions
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'''Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog''' | {{Structure | ||
|PDB= 2rft |SIZE=350|CAPTION= <scene name='initialview01'>2rft</scene>, resolution 2.80Å | |||
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+343'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+345'>AC2</scene>, <scene name='pdbsite=AC3:Nag+Binding+Site+For+Residue+A+346'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+A+347'>AC4</scene>, <scene name='pdbsite=AC5:Nag+Binding+Site+For+Residue+A+348'>AC5</scene>, <scene name='pdbsite=AC6:Nag+Binding+Site+For+Residue+A+349'>AC6</scene>, <scene name='pdbsite=AC7:Nag+Binding+Site+For+Residue+A+350'>AC7</scene>, <scene name='pdbsite=AC8:Nag+Binding+Site+For+Residue+A+351'>AC8</scene>, <scene name='pdbsite=AC9:Nag+Binding+Site+For+Residue+B+170'>AC9</scene>, <scene name='pdbsite=BC1:Sia+Binding+Site+For+Residue+A+3021'>BC1</scene>, <scene name='pdbsite=BC2:Bgc+Binding+Site+For+Residue+A+3025'>BC2</scene>, <scene name='pdbsite=BC3:Gal+Binding+Site+For+Residue+A+3024'>BC3</scene>, <scene name='pdbsite=BC4:Ndg+Binding+Site+For+Residue+A+3023'>BC4</scene> and <scene name='pdbsite=BC5:Gal+Binding+Site+For+Residue+A+3022'>BC5</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |||
|ACTIVITY= | |||
|GENE= Hemagglutinin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11520 Influenza B virus]) | |||
}} | |||
'''Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2RFT is a [ | 2RFT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_b_virus Influenza b virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RFT OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for receptor specificity of influenza B virus hemagglutinin., Wang Q, Tian X, Chen X, Ma J, Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16874-9. Epub 2007 Oct 17. PMID:[http:// | Structural basis for receptor specificity of influenza B virus hemagglutinin., Wang Q, Tian X, Chen X, Ma J, Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16874-9. Epub 2007 Oct 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17942670 17942670] | ||
[[Category: Influenza b virus]] | [[Category: Influenza b virus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: virion]] | [[Category: virion]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:35:43 2008'' | ||
Revision as of 19:35, 20 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | Hemagglutinin (Influenza B virus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of influenza B virus hemagglutinin in complex with LSTa receptor analog
OverviewOverview
Receptor-binding specificity of HA, the major surface glycoprotein of influenza virus, primarily determines the host ranges that the virus can infect. Influenza type B virus almost exclusively infects humans and contributes to the annual "flu" sickness. Here we report the structures of influenza B virus HA in complex with human and avian receptor analogs, respectively. These structures provide a structural basis for the different receptor-binding properties of influenza A and B virus HA molecules and for the ability of influenza B virus HA to distinguish human and avian receptors. The structure of influenza B virus HA with avian receptor analog also reveals how mutations in the region of residues 194 to 196, which are frequently observed in egg-adapted and naturally occurring variants, directly affect the receptor binding of the resultant virus strains. Furthermore, these structures of influenza B virus HA are compared with known structures of influenza A virus HAs, which suggests the role of the residue at 222 as a key and likely a universal determinant for the different binding modes of human receptor analogs by different HA molecules.
About this StructureAbout this Structure
2RFT is a Protein complex structure of sequences from Influenza b virus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for receptor specificity of influenza B virus hemagglutinin., Wang Q, Tian X, Chen X, Ma J, Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16874-9. Epub 2007 Oct 17. PMID:17942670
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