4ncu
From Proteopedia
(Difference between revisions)
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<StructureSection load='4ncu' size='340' side='right'caption='[[4ncu]], [[Resolution|resolution]] 1.11Å' scene=''> | <StructureSection load='4ncu' size='340' side='right'caption='[[4ncu]], [[Resolution|resolution]] 1.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ncu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCU OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4ncu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rfo|1rfo]], [[4ncv|4ncv]], [[4ncw|4ncw]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rfo|1rfo]], [[4ncv|4ncv]], [[4ncw|4ncw]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ncu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ncu OCA], [https://pdbe.org/4ncu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ncu RCSB], [https://www.ebi.ac.uk/pdbsum/4ncu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ncu ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | C3-Symmetric trimesic acid scaffolds, functionalized with bromoacetyl, aminooxyacetyl and azidoacetyl moieties, respectively, were synthesized and compared regarding their utility for the trivalent presentation of peptides using three different chemoselective ligation reactions, i.e. thioether and oxime formation, as well as the "click" reaction. The latter ligation method was then used to covalently stabilize the trimer of foldon, a 27 amino acid trimerization domain of bacteriophage T4 fibritin, by linking the three foldon monomers to the triazido-functionalized trimesic acid scaffold. This reaction dramatically enhanced the thermal stability of the trimer, while maintaining the correct fold, as demonstrated by CD spectroscopy and X-ray crystal structure analysis, respectively, of the foldon-scaffold conjugates. | ||
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| + | Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.,Berthelmann A, Lach J, Grawert MA, Groll M, Eichler J Org Biomol Chem. 2014 Apr 28;12(16):2606-14. doi: 10.1039/c3ob42251h. PMID:24637609<ref>PMID:24637609</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ncu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Fibritin|Fibritin]] | *[[Fibritin|Fibritin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:04, 25 August 2022
Foldon domain wild type
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