1v3d: Difference between revisions

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New page: left|200px<br /><applet load="1v3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v3d, resolution 2.28Å" /> '''Structure of the hem...
 
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[[Image:1v3d.gif|left|200px]]<br /><applet load="1v3d" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1v3d.gif|left|200px]]<br /><applet load="1v3d" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1v3d, resolution 2.28&Aring;" />
caption="1v3d, resolution 2.28&Aring;" />
'''Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2EN'''<br />
'''Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2EN'''<br />


==Overview==
==Overview==
The three-dimensional structure of the haemagglutinin-neuraminidase (HN), from a human parainfluenza virus is described at ca 2.0 A resolution, both, in native form and in complex with three substrate analogues. In support, of earlier work on the structure of the homologous protein from the avian, pathogen Newcastle disease virus (NDV), we observe a dimer of, beta-propellers and find no evidence for spatially separated sites, performing the receptor-binding and neuraminidase functions of the, protein. As with the NDV HN, the active site of the HN of parainfluenza, viruses is structurally flexible, suggesting that it may be able to switch, between a receptor-binding state and a catalytic state. However, in, contrast to the NDV structures, we observe no ligand-induced structural, changes that extend beyond the active site and modify the dimer interface.
The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface.


==About this Structure==
==About this Structure==
1V3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_parainfluenza_virus_4 Human parainfluenza virus 4] with NAG, CA, SO4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V3D OCA].  
1V3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_parainfluenza_virus_4 Human parainfluenza virus 4] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</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=1V3D OCA].  


==Reference==
==Reference==
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[[Category: Human parainfluenza virus 4]]
[[Category: Human parainfluenza virus 4]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Borg, N.A.]]
[[Category: Borg, N A.]]
[[Category: Colman, P.M.]]
[[Category: Colman, P M.]]
[[Category: Epa, V.C.]]
[[Category: Epa, V C.]]
[[Category: Lawrence, M.C.]]
[[Category: Lawrence, M C.]]
[[Category: McKimm-Breschkin, J.L.]]
[[Category: McKimm-Breschkin, J L.]]
[[Category: Pilling, P.A.]]
[[Category: Pilling, P A.]]
[[Category: Streltsov, V.A.]]
[[Category: Streltsov, V A.]]
[[Category: Varghese, J.N.]]
[[Category: Varghese, J N.]]
[[Category: CA]]
[[Category: CA]]
[[Category: DAN]]
[[Category: DAN]]
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[[Category: piv3 hn]]
[[Category: piv3 hn]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:33:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:31:03 2008''

Revision as of 16:31, 21 February 2008

File:1v3d.gif


1v3d, resolution 2.28Å

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Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type III: complex with NEU5AC2EN

OverviewOverview

The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface.

About this StructureAbout this Structure

1V3D is a Single protein structure of sequence from Human parainfluenza virus 4 with , , and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.

ReferenceReference

Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III., Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM, J Mol Biol. 2004 Jan 30;335(5):1343-57. PMID:14729348

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