2rfu
From Proteopedia
(New page: 200px<br /><applet load="2rfu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rfu" /> ''''''<br /> ==About this Structure== is a [h...) |
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[[Image:2rfu.jpg|left|200px]]<br /><applet load="2rfu" size="350" color="white" frame="true" align="right" spinBox="true" | [[Image:2rfu.jpg|left|200px]]<br /><applet load="2rfu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2rfu" /> | + | caption="2rfu, resolution 2.80Å" /> |
| - | ''''''<br /> | + | '''Crystal structure of influenza B virus hemagglutinin in complex with LSTc receptor analog'''<br /> |
| + | |||
| + | ==Overview== | ||
| + | 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 Structure== | ==About this Structure== | ||
| - | + | 2RFU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_b_virus Influenza b virus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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+347'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+A+349'>AC4</scene>, <scene name='pdbsite=AC5:Nag+Binding+Site+For+Residue+A+351'>AC5</scene>, <scene name='pdbsite=AC6:Nag+Binding+Site+For+Residue+B+170'>AC6</scene>, <scene name='pdbsite=AC7:Sia+Binding+Site+For+Residue+A+801'>AC7</scene>, <scene name='pdbsite=AC8:Nag+Binding+Site+For+Residue+A+803'>AC8</scene> and <scene name='pdbsite=AC9:Gal+Binding+Site+For+Residue+A+802'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RFU OCA]. | |
| + | |||
| + | ==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17942670 17942670] | ||
| + | [[Category: Influenza b virus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Chen, X.]] | ||
| + | [[Category: Ma, J.]] | ||
| + | [[Category: Tian, X.]] | ||
| + | [[Category: Wang, Q.]] | ||
| + | [[Category: NAG]] | ||
| + | [[Category: envelope protein]] | ||
| + | [[Category: fusion protein]] | ||
| + | [[Category: glycoprotein]] | ||
| + | [[Category: hemagglutinin]] | ||
| + | [[Category: human receptor analog]] | ||
| + | [[Category: influenza]] | ||
| + | [[Category: lipoprotein]] | ||
| + | [[Category: membrane]] | ||
| + | [[Category: palmitate]] | ||
| + | [[Category: receptor specificity]] | ||
| + | [[Category: transmembrane]] | ||
| + | [[Category: viral protein]] | ||
| + | [[Category: virion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:24:13 2008'' |
Revision as of 15:24, 6 February 2008
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Crystal structure of influenza B virus hemagglutinin in complex with LSTc receptor analog
Overview
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 Structure
2RFU is a Protein complex structure of sequences from Influenza b virus with as ligand. Known structural/functional Sites: , , , , , , , and . Full crystallographic information is available from OCA.
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:17942670
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