1e8v: Difference between revisions

Revision as of 00:20, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1e8v.png

Template:STRUCTURE 1e8v

STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASESTRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE

Template:ABSTRACT PUBMED 11062565

About this StructureAbout this Structure

1E8V is a Single protein structure of sequence from Newcastle disease virus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase., Crennell S, Takimoto T, Portner A, Taylor G, Nat Struct Biol. 2000 Nov;7(11):1068-74. PMID:11062565

Page seeded by OCA on Tue Jul 1 00:20:05 2008

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+===STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE===
-==Overview==
+<!--
-Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the beta-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a beta-propeller fold. Comparison of the structures of the two complexes reveal differences in the active site, suggesting that the catalytic site is activated by a conformational switch. This site may provide both sialic acid binding and hydrolysis functions since there is no evidence for a second sialic acid binding site in HN. Evidence for a single site with dual functions is examined and supported by mutagenesis studies. The structure provides the basis for the structure-based design of inhibitors for a range of paramyxovirus-induced diseases.
+The line below this paragraph, {{ABSTRACT_PUBMED_11062565}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11062565}}
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 [[Category: Neuraminidase]]
 [[Category: Sialidase]]
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