View source for 2rft

[[Image:2rft.jpg|left|200px]]

 {{Structure
|PDB= 2rft |SIZE=350|CAPTION= <scene name='initialview01'>2rft</scene>, resolution 2.80&Aring;
|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==
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==
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==
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: 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: 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 Thu Mar 20 18:35:43 2008''