2bat: Difference between revisions
New page: left|200px<br /><applet load="2bat" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bat, resolution 2.0Å" /> '''THE STRUCTURE OF THE ... |
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[[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size=" | [[Image:2bat.gif|left|200px]]<br /><applet load="2bat" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bat, resolution 2.0Å" /> | caption="2bat, resolution 2.0Å" /> | ||
'''THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR'''<br /> | '''THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
Crystallographic studies of neuraminidase-sialic acid complexes indicate | Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis. | ||
==About this Structure== | ==About this Structure== | ||
2BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, SIA 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:// | 2BAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SIA:'>SIA</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=2BAT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Colman, P | [[Category: Colman, P M.]] | ||
[[Category: Varghese, J | [[Category: Varghese, J N.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:47 2008'' | ||
Revision as of 17:35, 21 February 2008
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THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR
OverviewOverview
Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis.
About this StructureAbout this Structure
2BAT is a Single protein structure of sequence from [1] with , and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
ReferenceReference
The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor., Varghese JN, McKimm-Breschkin JL, Caldwell JB, Kortt AA, Colman PM, Proteins. 1992 Nov;14(3):327-32. PMID:1438172
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