2AFF
The solution structure of the Ki67FHA/hNIFK(226-269)3P complex
Summary for 2AFF
| Entry DOI | 10.2210/pdb2aff/pdb |
| Related | 1R21 |
| NMR Information | BMRB: 6748 |
| Descriptor | Antigen KI-67, MKI67 FHA domain interacting nucleolar phosphoprotein (2 entities in total) |
| Functional Keywords | ki67; fha; nifk; nmr; phosphoprotein, cell cycle |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P46013 Nucleus, nucleolus: Q9BYG3 |
| Total number of polymer chains | 2 |
| Total formula weight | 19024.21 |
| Authors | Byeon, I.-J.L.,Li, H.,Song, H.,Gronenborn, A.M.,Tsai, M.D. (deposition date: 2005-07-25, release date: 2005-10-25, Last modification date: 2024-10-30) |
| Primary citation | Byeon, I.J.,Li, H.,Song, H.,Gronenborn, A.M.,Tsai, M.D. Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. Nat.Struct.Mol.Biol., 12:987-993, 2005 Cited by PubMed Abstract: The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. We have determined the solution structure of Ki67FHA in complex with the triply phosphorylated peptide hNIFK226-269(3P), revealing not only local recognition of pThr234 but also the extension of the beta-sheet of the FHA domain by the addition of a beta-strand of hNIFK. The structure of an FHA domain in complex with a biologically relevant binding partner provides insights into ligand specificity and potentially links the cancer marker protein Ki67 to a signaling pathway associated with cell fate specification. PubMed: 16244663DOI: 10.1038/nsmb1008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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