1e8v
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1e8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8v, resolution 2.0Å" /> '''STRUCTURE OF THE MULT...)
Next diff →
Revision as of 11:42, 20 November 2007
|
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.
About this Structure
1E8V is a Single protein structure of sequence from Newcastle disease virus with NDG, NAG, CA and DAN as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
Reference
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 Nov 20 13:50:03 2007
