2lms

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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...)
Current revision (06:11, 27 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2lms is ON HOLD
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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==
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<StructureSection load='2lms' size='340' side='right'caption='[[2lms]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Ghasriani, H., Belcourt, P., Sauve, S., Hodgson, D.J., Gingras, G., Brochu, D., Gilbert, M., Aubin, Y.
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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>
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Description: 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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2lms" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Interferon 3D structures|Interferon 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Aubin Y]]
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[[Category: Belcourt PJF]]
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[[Category: Brochu D]]
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[[Category: Ghasriani H]]
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[[Category: Gilbert M]]
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[[Category: Gingras G]]
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[[Category: Hodgson DJ]]
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[[Category: Sauve S]]

Current revision

A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site

PDB ID 2lms

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