1z4y: Difference between revisions

Revision as of 17:12, 21 February 2008

Parainfluenza Virus 5 (SV5) Hemagglutinin-Neuraminidase (HN) (pH 8.0)

OverviewOverview

The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus attachment to cells, cleavage of sialic acid from oligosaccharides, and stimulating membrane fusion during virus entry into cells. The structural basis for these diverse functions remains to be fully understood. We report the crystal structures of the parainfluenza virus 5 (SV5) HN and its complexes with sialic acid, the inhibitor DANA, and the receptor sialyllactose. SV5 HN shares common structural features with HN of Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but unlike the previously determined HN structures, the SV5 HN forms a tetramer in solution, which is thought to be the physiological oligomer. The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures do not support previously proposed models for HN action in membrane fusion and suggest alternative mechanisms by which HN may promote virus entry into cells.

About this StructureAbout this Structure

1Z4Y is a Single protein structure of sequence from Simian virus 5 with and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose., Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS, Structure. 2005 May;13(5):803-15. PMID:15893670

Page seeded by OCA on Thu Feb 21 16:12:09 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1z4y.gif|left|200px]]<br /><applet load="1z4y" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1z4y.gif|left|200px]]<br /><applet load="1z4y" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1z4y, resolution 2.600&Aring;" />
 '''Parainfluenza Virus 5 (SV5) Hemagglutinin-Neuraminidase (HN) (pH 8.0)'''<br />
 ==Overview==
-The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus, attachment to cells, cleavage of sialic acid from oligosaccharides, and, stimulating membrane fusion during virus entry into cells. The structural, basis for these diverse functions remains to be fully understood. We, report the crystal structures of the parainfluenza virus 5 (SV5) HN and, its complexes with sialic acid, the inhibitor DANA, and the receptor, sialyllactose. SV5 HN shares common structural features with HN of, Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but, unlike the previously determined HN structures, the SV5 HN forms a, tetramer in solution, which is thought to be the physiological oligomer., The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures, do not support previously proposed models for HN action in membrane fusion, and suggest alternative mechanisms by which HN may promote virus entry, into cells.
+The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus attachment to cells, cleavage of sialic acid from oligosaccharides, and stimulating membrane fusion during virus entry into cells. The structural basis for these diverse functions remains to be fully understood. We report the crystal structures of the parainfluenza virus 5 (SV5) HN and its complexes with sialic acid, the inhibitor DANA, and the receptor sialyllactose. SV5 HN shares common structural features with HN of Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but unlike the previously determined HN structures, the SV5 HN forms a tetramer in solution, which is thought to be the physiological oligomer. The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures do not support previously proposed models for HN action in membrane fusion and suggest alternative mechanisms by which HN may promote virus entry into cells.
 ==About this Structure==
-Z4Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_5 Simian virus 5] with NDG and CA 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=1Z4Y OCA].
+Z4Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_5 Simian virus 5] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=CA:'>CA</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=1Z4Y OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Simian virus 5]]
 [[Category: Single protein]]
-[[Category: Jardetzky, T.S.]]
+[[Category: Jardetzky, T S.]]
-[[Category: Lamb, R.A.]]
+[[Category: Lamb, R A.]]
-[[Category: Paterson, R.G.]]
+[[Category: Paterson, R G.]]
-[[Category: Thompson, T.B.]]
+[[Category: Thompson, T B.]]
-[[Category: Wurzburg, B.A.]]
+[[Category: Wurzburg, B A.]]
 [[Category: Yuan, P.]]
 [[Category: CA]]
@@ Line 27: / Line 27: @@
 [[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:14:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:09 2008''