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2l9i
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of thymosin alpha-1== | |
| + | <StructureSection load='2l9i' size='340' side='right'caption='[[2l9i]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l9i]] 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=2L9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9I FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=2l9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9i OCA], [https://pdbe.org/2l9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9i RCSB], [https://www.ebi.ac.uk/pdbsum/2l9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PTMA_HUMAN PTMA_HUMAN] Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 800MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double beta-turns in the N-terminal twelve residues which form a distorted helical structure. | ||
| - | + | NMR structure of human thymosin alpha-1.,Elizondo-Riojas MA, Chamow SM, Tuthill CW, Gorenstein DG, Volk DE Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):356-61. Epub 2011 Nov 15. PMID:22115779<ref>PMID:22115779</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2l9i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Elizondo-Riojas MA]] | ||
| + | [[Category: Gorenstein DG]] | ||
| + | [[Category: Volk DE]] | ||
Current revision
NMR structure of thymosin alpha-1
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