4X9V
PLK-1 polo-box domain in complex with Bioactive Imidazolium-containing phosphopeptide macrocycle 3C
Summary for 4X9V
Entry DOI | 10.2210/pdb4x9v/pdb |
Related | 4X9R 4X9W |
Descriptor | Serine/threonine-protein kinase PLK1, Phosphopeptide macrocycle 3C (3 entities in total) |
Functional Keywords | macrocycle inhibitor complex, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus: P53350 |
Total number of polymer chains | 2 |
Total formula weight | 28273.30 |
Authors | Grant, R.A.,Qian, W.-J.,Yaffe, M.B.,Burke, T.R. (deposition date: 2014-12-11, release date: 2015-07-29, Last modification date: 2024-10-23) |
Primary citation | Qian, W.J.,Park, J.E.,Grant, R.,Lai, C.C.,Kelley, J.A.,Yaffe, M.B.,Lee, K.S.,Burke, T.R. Neighbor-directed histidine N ( tau )-alkylation: A route to imidazolium-containing phosphopeptide macrocycles. Biopolymers, 104:663-673, 2015 Cited by PubMed Abstract: Our recently discovered, selective, on-resin route to N(τ)-alkylated imidazolium-containing histidine residues affords new strategies for peptide mimetic design. In this, we demonstrate the use of this chemistry to prepare a series of macrocyclic phosphopeptides, in which imidazolium groups serve as ring-forming junctions. Interestingly, these cationic moieties subsequently serve to charge-mask the phosphoamino acid group that directed their formation. Neighbor-directed histidine N(τ)-alkylation opens the door to new families of phosphopeptidomimetics for use in a range of chemical biology contexts. PubMed: 26152807DOI: 10.1002/bip.22698 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.429 Å) |
Structure validation
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