1nsb: Difference between revisions

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-[[Image:1nsb.png|left|200px]]
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+==THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID==
-The line below this paragraph, containing "STRUCTURE_1nsb", creates the "Structure Box" on the page.
+<StructureSection load='1nsb' size='340' side='right'caption='[[1nsb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1nsb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(STRAIN_B/BEIJING/1/87) Influenza B virus (STRAIN B/BEIJING/1/87)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_1nsb|  PDB=1nsb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsb OCA], [https://pdbe.org/1nsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsb RCSB], [https://www.ebi.ac.uk/pdbsum/1nsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NRAM_INBBE NRAM_INBBE] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Influenza virus neuraminidase catalyses the cleavage of terminal sialic acid, the viral receptor, from carbohydrate chains on glycoproteins and glycolipids. We present the crystal structure of the enzymatically active head of influenza B virus neuraminidase from the strain B/Beijing/1/87. The native structure has been refined to a crystallographic R-factor of 14.8% at 2.2 A resolution and its complex with sialic acid refined at 2.8 A resolution. The overall fold of the molecule is very similar to the already known structure of neuraminidase from influenza A virus, with which there is amino acid sequence homology of approximately 30%. Two calcium binding sites have been identified. One of them, previously undescribed, is located between the active site and a large surface antigenic loop. The calcium ion is octahedrally co-ordinated by five oxygen atoms from the protein and one water molecule. Sequence comparisons suggest that this calcium site should occur in all influenza A and B virus neuraminidases. Soaking of sialic acid into the crystals has enabled the mode of binding of the reaction product in the putative active site pocket to be revealed. All the large side groups of the sialic acid are equatorial and are specifically recognized by nine fully conserved active site residues. These in turn are stabilized by a second shell of 10 highly conserved residues principally by an extensive network of hydrogen bonds.
-===THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID===
+The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid.,Burmeister WP, Ruigrok RW, Cusack S EMBO J. 1992 Jan;11(1):49-56. PMID:1740114<ref>PMID:1740114</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_1740114}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1nsb" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 1740114 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_1740114}}
-==About this Structure==
-[[1nsb]] is a 2 chain structure of [[Neuraminidase]] with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSB OCA].
 ==See Also==
-*[[Neuraminidase]]
+*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:001740114</ref><references group="xtra"/>
+__TOC__
-[[Category: Exo-alpha-sialidase]]
+</StructureSection>
-[[Category: Viruses]]
+[[Category: Large Structures]]
-[[Category: Burmeister, W P.]]
+[[Category: Burmeister WP]]
-[[Category: Cusack, S.]]
+[[Category: Cusack S]]
-[[Category: Ruigrok, R W.H.]]
+[[Category: Ruigrok RWH]]