2lms: Difference between revisions
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New page: '''Unreleased structure''' The entry 2lms is ON HOLD Authors: Ghasriani, H., Belcourt, P., Sauve, S., Hodgson, D.J., Gingras, G., Brochu, D., Gilbert, M., Aubin, Y. Description: A sing... |
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==A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site== | |||
<StructureSection load='2lms' size='340' side='right'caption='[[2lms]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lms]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LMS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lms OCA], [https://pdbe.org/2lms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lms RCSB], [https://www.ebi.ac.uk/pdbsum/2lms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lms ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymatic addition of GalNAc to isotopically labeled IFNalpha2a produced in Escherichia coli yielded the O-linked glycoprotein GalNAcalpha-[(13)C,(15)N]IFNalpha2a. The three-dimensional structure of GalNAcalpha-IFNalpha2a has been determined in solution by NMR spectroscopy at high resolution. Proton-nitrogen heteronuclear Overhauser enhancement measurements revealed that the addition of a single monosaccharide unit at Thr-106 significantly slowed motions of the glycosylation loop on the nanosecond time scale. Subsequent addition of a Gal unit produced Gal(beta1,3)GalNAcalpha-[(13)C,(15)N]IFNalpha2a. This extension resulted in a further decrease in the dynamics of this loop. The methodology used here allowed the first such description of the structure and dynamics of an O-glycoprotein and opens the way to the study of this class of proteins. | |||
A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site.,Ghasriani H, Belcourt PJ, Sauve S, Hodgson DJ, Brochu D, Gilbert M, Aubin Y J Biol Chem. 2013 Jan 4;288(1):247-54. doi: 10.1074/jbc.M112.413252. Epub 2012, Nov 26. PMID:23184955<ref>PMID:23184955</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lms" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interferon 3D structures|Interferon 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Aubin Y]] | |||
[[Category: Belcourt PJF]] | |||
[[Category: Brochu D]] | |||
[[Category: Ghasriani H]] | |||
[[Category: Gilbert M]] | |||
[[Category: Gingras G]] | |||
[[Category: Hodgson DJ]] | |||
[[Category: Sauve S]] | |||
Latest revision as of 06:11, 27 November 2024
A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site
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