1nsd: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1nsd.png|left|200px]]
-<!--
+==INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR==
-The line below this paragraph, containing "STRUCTURE_1nsd", creates the "Structure Box" on the page.
+<StructureSection load='1nsd' size='340' side='right'caption='[[1nsd]], [[Resolution|resolution]] 1.80&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'>[[1nsd]] 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=1NSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSD 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]] 1.8&#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=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_1nsd|  PDB=1nsd  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsd OCA], [https://pdbe.org/1nsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsd RCSB], [https://www.ebi.ac.uk/pdbsum/1nsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsd 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 ==
+BACKGROUND: Neuraminidase, one of the two surface glycoproteins of influenza virus, cleaves terminal sialic acid residues from glycolipids or glycoproteins. Its crystal structure is known at high resolution, but the mechanism of glycosyl hydrolysis remains unclear. RESULTS: We have determined the crystal structure at 1.8 A resolution of two complexes of influenza B/Beijing neuraminidase containing either the reaction product, sialic acid, or the transition state analogue inhibitor, 2,3-dehydro-2-deoxy-N-acetylneuraminic acid (DANA). The sialic acid is bound in a distorted 'boat' conformation closely resembling that of bound DANA, stabilized by a conserved tyrosine residue (Tyr408). This distortion also gives rise to a suicidal side reaction that converts sialic acid to DANA at a low rate. CONCLUSIONS: The mechanism of neuraminidase action is distinct from that of other known glycosyl hydrolases. Substrate distortion appears to be the driving force in glycosyl bond hydrolysis and the proton required for catalysis can probably be donated by water, rather than by residues in the active site, thus allowing the enzyme to operate at high pH. The side reaction converting sialic acid to DANA appears reasonably favourable, and it is unclear how this is minimized by the enzyme.
-===INFLUENZA B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR===
+Influenza B virus neuraminidase can synthesize its own inhibitor.,Burmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RW Structure. 1993 Sep 15;1(1):19-26. PMID:8069621<ref>PMID:8069621</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1nsd" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8069621}}, adds the Publication Abstract to the page
+*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8069621 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8069621}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-NSD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_b_virus Influenza b virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSD OCA].
+[[Category: Burmeister WP]]
+[[Category: Cusack S]]
-==Reference==
+[[Category: Ruigrok RWH]]
-Influenza B virus neuraminidase can synthesize its own inhibitor., Burmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RW, Structure. 1993 Sep 15;1(1):19-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8069621 8069621]
-[[Category: Exo-alpha-sialidase]]
-[[Category: Influenza b virus]]
-[[Category: Single protein]]
-[[Category: Burmeister, W P.]]
-[[Category: Cusack, S.]]
-[[Category: Ruigrok, R W.H.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:55:41 2008''