5nn9

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(New page: 200px<br /><applet load="5nn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="5nn9, resolution 2.3&Aring;" /> '''REFINED ATOMIC STRUCT...)
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[[Image:5nn9.gif|left|200px]]<br /><applet load="5nn9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="5nn9, resolution 2.3&Aring;" />
caption="5nn9, resolution 2.3&Aring;" />
'''REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS'''<br />
'''REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS'''<br />
==Overview==
==Overview==
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The crystal structure of the N9 subtype neuraminidase of influenza virus, was refined by simulated annealing and conventional techniques to an, R-factor of 0.172 for data in the resolution range 6.0 to 2.2 A. The, r.m.s. deviation from ideal values of bond lengths is 0.014 A. The, structure is similar to that of N2 subtype neuraminidase both in secondary, structure elements and in their connections. The three-dimensional, structures of several escape mutants of neuraminidase, selected with, antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the, mutation site or to residues that are spatially immediately adjacent to, it. The failure of antisera to cross-react between N2 and N9 subtypes may, be correlated with the absence of conserved, contiguous surface structures, of area 700 A2 or more.
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The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0.172 for data in the resolution range 6.0 to 2.2 A. The r.m.s. deviation from ideal values of bond lengths is 0.014 A. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 A2 or more.
==About this Structure==
==About this Structure==
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5NN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus] with NAG 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=5NN9 OCA].
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5NN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus] with <scene name='pdbligand=NAG:'>NAG</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=5NN9 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Unidentified influenza virus]]
[[Category: Unidentified influenza virus]]
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[[Category: Baker, A.T.]]
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[[Category: Baker, A T.]]
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[[Category: Colman, P.M.]]
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[[Category: Colman, P M.]]
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[[Category: Laver, W.G.]]
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[[Category: Laver, W G.]]
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[[Category: Tulip, W.R.]]
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[[Category: Tulip, W R.]]
[[Category: Vandonkelaar, A.]]
[[Category: Vandonkelaar, A.]]
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[[Category: Varghese, J.N.]]
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[[Category: Varghese, J N.]]
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[[Category: Webster, R.G.]]
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[[Category: Webster, R G.]]
[[Category: CA]]
[[Category: CA]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: hydrolase(o-glycosyl)]]
[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:37:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:33 2008''

Revision as of 17:15, 21 February 2008


5nn9, resolution 2.3Å

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REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS

Overview

The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0.172 for data in the resolution range 6.0 to 2.2 A. The r.m.s. deviation from ideal values of bond lengths is 0.014 A. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 A2 or more.

About this Structure

5NN9 is a Single protein structure of sequence from Unidentified influenza 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

Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants., Tulip WR, Varghese JN, Baker AT, van Donkelaar A, Laver WG, Webster RG, Colman PM, J Mol Biol. 1991 Sep 20;221(2):487-97. PMID:1920429

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