5nn9: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image: | ==REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS== | ||
<StructureSection load='5nn9' size='340' side='right' caption='[[5nn9]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nn9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NN9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5nn9 RCSB], [http://www.ebi.ac.uk/pdbsum/5nn9 PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/5nn9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:1920429</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Neuraminidase|Neuraminidase]] | *[[Neuraminidase|Neuraminidase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
[[Category: Baker, A T | [[Category: Baker, A T]] | ||
[[Category: Colman, P M | [[Category: Colman, P M]] | ||
[[Category: Laver, W G | [[Category: Laver, W G]] | ||
[[Category: Tulip, W R | [[Category: Tulip, W R]] | ||
[[Category: Vandonkelaar, A | [[Category: Vandonkelaar, A]] | ||
[[Category: Varghese, J N | [[Category: Varghese, J N]] | ||
[[Category: Webster, R G | [[Category: Webster, R G]] |
Revision as of 19:55, 10 December 2014
REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTSREFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|