4xl8: Difference between revisions
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==Crystal Structure of Human Adenovirus 52 Short Fiber Knob in Complex with 2-O-Methyl-5-N-Acetylneuraminic Acid== | ==Crystal Structure of Human Adenovirus 52 Short Fiber Knob in Complex with 2-O-Methyl-5-N-Acetylneuraminic Acid== | ||
<StructureSection load='4xl8' size='340' side='right' caption='[[4xl8]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='4xl8' size='340' side='right'caption='[[4xl8]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xl8]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XL8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xl8]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Adenovirus_52 Adenovirus 52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XL8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MNA:2-O-METHYL-5-N-ACETYL-ALPHA-D-+NEURAMINIC+ACID'>MNA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MNA:2-O-METHYL-5-N-ACETYL-ALPHA-D-+NEURAMINIC+ACID'>MNA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></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=4xl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl8 OCA], [http://pdbe.org/4xl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4xl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xl8 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=4xl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xl8 OCA], [http://pdbe.org/4xl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4xl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xl8 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Adenovirus 52]] | |||
[[Category: Large Structures]] | |||
[[Category: Liaci, A M]] | [[Category: Liaci, A M]] | ||
[[Category: Stehle, T]] | [[Category: Stehle, T]] | ||
Revision as of 10:11, 29 May 2019
Crystal Structure of Human Adenovirus 52 Short Fiber Knob in Complex with 2-O-Methyl-5-N-Acetylneuraminic AcidCrystal Structure of Human Adenovirus 52 Short Fiber Knob in Complex with 2-O-Methyl-5-N-Acetylneuraminic Acid
Structural highlights
Publication Abstract from PubMedMost adenoviruses attach to host cells by means of the protruding fiber protein that binds to host cells via the coxsackievirus and adenovirus receptor (CAR) protein. Human adenovirus type 52 (HAdV-52) is one of only three gastroenteritis-causing HAdVs that are equipped with two different fiber proteins, one long and one short. Here we show, by means of virion-cell binding and infection experiments, that HAdV-52 can also attach to host cells via CAR, but most of the binding depends on sialylated glycoproteins. Glycan microarray, flow cytometry, surface plasmon resonance and ELISA analyses reveal that the terminal knob domain of the long fiber (52LFK) binds to CAR, and the knob domain of the short fiber (52SFK) binds to sialylated glycoproteins. X-ray crystallographic analysis of 52SFK in complex with 2-O-methylated sialic acid combined with functional studies of knob mutants revealed a new sialic acid binding site compared to other, known adenovirus:glycan interactions. Our findings shed light on adenovirus biology and may help to improve targeting of adenovirus-based vectors for gene therapy. Human Adenovirus 52 Uses Sialic Acid-containing Glycoproteins and the Coxsackie and Adenovirus Receptor for Binding to Target Cells.,Lenman A, Liaci AM, Liu Y, Ardahl C, Rajan A, Nilsson E, Bradford W, Kaeshammer L, Jones MS, Frangsmyr L, Feizi T, Stehle T, Arnberg N PLoS Pathog. 2015 Feb 12;11(2):e1004657. doi: 10.1371/journal.ppat.1004657., eCollection 2015 Feb. PMID:25674795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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