1e8v
From Proteopedia
(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...) |
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| - | [[Image:1e8v.gif|left|200px]]<br /><applet load="1e8v" size=" | + | [[Image:1e8v.gif|left|200px]]<br /><applet load="1e8v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e8v, resolution 2.0Å" /> | caption="1e8v, resolution 2.0Å" /> | ||
'''STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE'''<br /> | '''STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Paramyxoviruses are the main cause of respiratory disease in children. One | + | 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== | ==About this Structure== | ||
| - | 1E8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Newcastle_disease_virus Newcastle disease virus] with NDG, NAG, CA and DAN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http:// | + | 1E8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Newcastle_disease_virus Newcastle disease virus] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DAN:'>DAN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sialidase]] | [[Category: sialidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:18 2008'' |
Revision as of 10:25, 21 February 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.
About this Structure
1E8V 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 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
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