2AFF

The solution structure of the Ki67FHA/hNIFK(226-269)3P complex


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 512 
  • Conformers Submitted: 100 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.

Byeon, I.J.Li, H.Song, H.Gronenborn, A.M.Tsai, M.D.

(2005) Nat Struct Mol Biol 12: 987-993

  • DOI: https://doi.org/10.1038/nsmb1008
  • Primary Citation of Related Structures:  
    2AFF

  • 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.


  • Organizational Affiliation

    Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health (NIH), Bethesda, Maryland 20892, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Antigen KI-67120Homo sapiensMutation(s): 0 
Gene Names: MKI67
UniProt & NIH Common Fund Data Resources
Find proteins for P46013 (Homo sapiens)
Explore P46013 
Go to UniProtKB:  P46013
PHAROS:  P46013
GTEx:  ENSG00000148773 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46013
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
MKI67 FHA domain interacting nucleolar phosphoprotein44Homo sapiensMutation(s): 0 
Gene Names: MKI67IP
UniProt & NIH Common Fund Data Resources
Find proteins for Q9BYG3 (Homo sapiens)
Explore Q9BYG3 
Go to UniProtKB:  Q9BYG3
PHAROS:  Q9BYG3
GTEx:  ENSG00000155438 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9BYG3
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  2 Unique
IDChains TypeFormula2D DiagramParent
SEP
Query on SEP
B
L-PEPTIDE LINKINGC3 H8 N O6 PSER
TPO
Query on TPO
B
L-PEPTIDE LINKINGC4 H10 N O6 PTHR
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 512 
  • Conformers Submitted: 100 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-10-25
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-09
    Changes: Data collection, Database references, Derived calculations