2vsk
From Proteopedia
(Difference between revisions)
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- | + | ==HENDRA VIRUS ATTACHMENT GLYCOPROTEIN IN COMPLEX WITH HUMAN CELL SURFACE RECEPTOR EPHRINB2== | |
- | + | <StructureSection load='2vsk' size='340' side='right' caption='[[2vsk]], [[Resolution|resolution]] 3.30Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[2vsk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hendra_virus Hendra virus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VSK FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vsm|2vsm]]</td></tr> | ||
+ | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vsk RCSB], [http://www.ebi.ac.uk/pdbsum/2vsk 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/vs/2vsk_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 == | ||
+ | Nipah and Hendra viruses are emergent paramyxoviruses, causing disease characterized by rapid onset and high mortality rates, resulting in their classification as Biosafety Level 4 pathogens. Their attachment glycoproteins are essential for the recognition of the cell-surface receptors ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3). Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2. In contrast to previously solved paramyxovirus attachment complexes, which are mediated by sialic acid interactions, the Nipah and Hendra complexes are maintained by an extensive protein-protein interface, including a crucial phenylalanine side chain on EFNB2 that fits snugly into a hydrophobic pocket on the viral protein. By analogy with the development of antivirals against sialic acid binding viruses, these results provide a structural template to target antiviral inhibition of protein-protein interactions. | ||
- | + | Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2.,Bowden TA, Aricescu AR, Gilbert RJ, Grimes JM, Jones EY, Stuart DI Nat Struct Mol Biol. 2008 Jun;15(6):567-72. Epub 2008 May 18. PMID:18488039<ref>PMID:18488039</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
+ | *[[Ephrin|Ephrin]] | ||
*[[Ephrin receptor|Ephrin receptor]] | *[[Ephrin receptor|Ephrin receptor]] | ||
*[[Hemagglutinin|Hemagglutinin]] | *[[Hemagglutinin|Hemagglutinin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Exo-alpha-sialidase]] | [[Category: Exo-alpha-sialidase]] | ||
[[Category: Hendra virus]] | [[Category: Hendra virus]] |
Revision as of 01:41, 1 October 2014
HENDRA VIRUS ATTACHMENT GLYCOPROTEIN IN COMPLEX WITH HUMAN CELL SURFACE RECEPTOR EPHRINB2
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Categories: Exo-alpha-sialidase | Hendra virus | Homo sapiens | Aricescu, A R. | Bowden, T A. | Gilbert, R J. | Grimes, J M. | Jones, E Y. | Stuart, D I. | B2 | Cell surface receptor | Complex | Developmental protein | Differentiation | Efn | Envelope protein | Eph | Ephrin | Glycoprotein | Hemagglutinin | Hendra | Henipavirus | Hev | Hev-g | Hydrolase | Membrane | Neurogenesis | Nipah | Niv | Niv-g | Paramyxovirus | Phosphoprotein | Signal-anchor | Transmembrane | Viral attachment | Virion | Virus