1usx: Difference between revisions

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~~'''~~CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE~~'''~~

===CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE===

~~==Overview==~~

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~~Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein~~, the ~~hemagglutinin-neuraminidase (HN), that is involved in attachment~~ to ~~sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus~~ (~~NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state~~. ~~Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion~~. ~~Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers~~, ~~perhaps indicative of the tetramer association found on~~ the ~~viral surface~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15016893}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15016893 is the PubMed ID number.

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==About this Structure==

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[[Category: Neuraminidase]]

[[Category: Sialidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 11~~:38:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:15:43 2008''

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-[[Image:1usx.gif|left|200px]]
+{{Seed}}
+[[Image:1usx.png|left|200px]]
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 {{STRUCTURE_1usx|  PDB=1usx  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE'''
+===CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE===
-==Overview==
+<!--
-Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.
+The line below this paragraph, {{ABSTRACT_PUBMED_15016893}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15016893 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15016893}}
 ==About this Structure==
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 [[Category: Neuraminidase]]
 [[Category: Sialidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:38:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:15:43 2008''