1usx: Difference between revisions

Revision as of 16:27, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1USX is a Single protein structure of sequence from Newcastle disease virus with , and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion., Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G, J Virol. 2004 Apr;78(7):3733-41. PMID:15016893

Page seeded by OCA on Thu Feb 21 15:27:54 2008

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@@ Line 4: / Line 4: @@
 ==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.
+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.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Groves, D.]]
-[[Category: Itzstein, M.Von.]]
+[[Category: Itzstein, M Von.]]
 [[Category: Kiefel, M.]]
 [[Category: Portner, A.]]
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 [[Category: sialidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:04:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:54 2008''