5nbh
From Proteopedia
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<StructureSection load='5nbh' size='340' side='right' caption='[[5nbh]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5nbh' size='340' side='right' caption='[[5nbh]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5nbh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nbh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Murine_adenovirus_2 Murine adenovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5n83|5n83]], [[5n8d|5n8d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5n83|5n83]], [[5n8d|5n8d]]</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=5nbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbh OCA], [http://pdbe.org/5nbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbh RCSB], [http://www.ebi.ac.uk/pdbsum/5nbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbh ProSAT]</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=5nbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbh OCA], [http://pdbe.org/5nbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbh RCSB], [http://www.ebi.ac.uk/pdbsum/5nbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Murine adenovirus 2 (MAdV-2) infects cells of the mouse gastrointestinal tract. Like human adenoviruses, it is a member of the genus Mastadenovirus, family Adenoviridae. The MAdV-2 genome has a single fibre gene that expresses a 787 residue-long protein. Through analogy to other adenovirus fibre proteins, it is expected that the carboxy-terminal virus-distal head domain of the fibre is responsible for binding to the host cell, although the natural receptor is unknown. The putative head domain has little sequence identity to adenovirus fibres of known structure. In this report, we present high-resolution crystal structures of the carboxy-terminal part of the MAdV-2 fibre. The structures reveal a domain with the typical adenovirus fibre head topology and a domain containing two triple beta-spiral repeats of the shaft domain. Through glycan microarray profiling, saturation transfer difference nuclear magnetic resonance spectroscopy, isothermal titration calorimetry and site-directed mutagenesis, we show that the fibre specifically binds to the monosaccharide N-acetylglucosamine (GlcNAc). The crystal structure of the complex reveals that GlcNAc binds between the AB and CD loops at the top of each of the three monomers of the MAdV-2 fibre head. However, infection competition assays show that soluble GlcNAc monosaccharide and natural GlcNAc-containing polymers do not inhibit infection by MAdV-2. Furthermore, site-directed mutation of the GlcNAc-binding residues does not prevent the inhibition of infection by soluble fibre protein. On the other hand, we show that the MAdV-2 fibre protein binds GlcNAc-containing mucin glycans, which suggests that the MAdV-2 fibre protein may play a role in viral mucin penetration in the mouse gut. | ||
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| + | Structure and N-acetylglucosamine binding of the distal domain of mouse adenovirus 2 fibre.,Singh AK, Nguyen TH, Vidovszky MZ, Harrach B, Benko M, Kirwan A, Joshi L, Kilcoyne M, Berbis MA, Canada FJ, Jimenez-Barbero J, Menendez M, Wilson SS, Bromme BA, Smith JG, van Raaij MJ J Gen Virol. 2018 Oct 2. doi: 10.1099/jgv.0.001145. PMID:30277856<ref>PMID:30277856</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5nbh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Murine adenovirus 2]] | ||
[[Category: Raaij, M J.van]] | [[Category: Raaij, M J.van]] | ||
[[Category: Singh, A K]] | [[Category: Singh, A K]] | ||
Revision as of 08:23, 10 October 2018
Structure of the distal domain of mouse adenovirus 2 fibre, P212121 native
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