4NCU
Foldon domain wild type
Summary for 4NCU
| Entry DOI | 10.2210/pdb4ncu/pdb |
| Related | 1RFO 4NCV 4NCW |
| Descriptor | Fibritin (2 entities in total) |
| Functional Keywords | trimeric scaffold, viral protein |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 3084.46 |
| Authors | Graewert, M.A.,Reiner, A.,Groll, M.,Kiefhaber, T. (deposition date: 2013-10-25, release date: 2014-03-05, 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 Cited by 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: 24637609DOI: 10.1039/c3ob42251h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.11 Å) |
Structure validation
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