2lms: Difference between revisions
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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lms]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LMS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2lms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lms OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lms RCSB], [http://www.ebi.ac.uk/pdbsum/2lms PDBsum]</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> | ||
==See Also== | |||
*[[Interferon|Interferon]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Aubin, Y | [[Category: Aubin, Y]] | ||
[[Category: Belcourt, P J.F | [[Category: Belcourt, P J.F]] | ||
[[Category: Brochu, D | [[Category: Brochu, D]] | ||
[[Category: Ghasriani, H | [[Category: Ghasriani, H]] | ||
[[Category: Gilbert, M | [[Category: Gilbert, M]] | ||
[[Category: Gingras, G | [[Category: Gingras, G]] | ||
[[Category: Hodgson, D J | [[Category: Hodgson, D J]] | ||
[[Category: Sauve, S | [[Category: Sauve, S]] | ||
[[Category: Cytokine]] | [[Category: Cytokine]] | ||
[[Category: Glycoprotein]] | [[Category: Glycoprotein]] | ||
Revision as of 11:43, 18 December 2014
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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