4ncu | pdb_00004ncu

Foldon domain wild type

spinqualitylabelsall models 4ncu, resolution 1.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ncu is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1rfo, 4ncv, 4ncw Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fibritin

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