4NCV

Foldon domain wild type N-conjugate

Summary for 4NCV

• Entry DOI: 10.2210/pdb4ncv/pdb
• Related: 1FRO 4NCU 4NCW
• Descriptor: Fibritin (2 entities in total)
• Functional Keywords: trimeric scaffold, chemical ligation, folding, trazido-functionalized trimesic acid scaffold, viral protein
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 3
• Total formula weight: 9331.50

Authors

Graewert, M.A.,Berthelmann, A.,Lach, J.,Groll, M.,Eichler, J. (deposition date: 2013-10-25, release date: 2014-03-12, Last modification date: 2023-09-20)

Primary citation

Berthelmann, A.,Lach, J.,Grawert, M.A.,Groll, M.,Eichler, J.
Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.
Org.Biomol.Chem., 12:2606-2614, 2014

PubMed Abstract: 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.

PubMed: 24637609
DOI: 10.1039/c3ob42251h

Experimental method

X-RAY DIFFRACTION (1.2 Å)