1A5E

SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 18 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 90 
  • Conformers Submitted: 18 
  • Selection Criteria: CLOSEST TO MEAN STRUCTURE WHICH SHOWS GOOD AGREEMENT WITH THE CONSTRAINTS. NONE OF THE CONSTRAINTS SHOW NOE VIOLATION BIGGER THAN 0.5 A AND DIHEDRAL ANGLE VIOLATION BIGGER THAN 5 DEGREE. 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Tumor suppressor p16INK4A: determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4.

Byeon, I.J.Li, J.Ericson, K.Selby, T.L.Tevelev, A.Kim, H.J.O'Maille, P.Tsai, M.D.

(1998) Mol Cell 1: 421-431

  • DOI: https://doi.org/10.1016/s1097-2765(00)80042-8
  • Primary Citation of Related Structures:  
    1A5E, 2A5E

  • PubMed Abstract: 

    The solution structure of the tumor suppressor p16INK4A has been determined by NMR, and important recognition regions of both cdk4 and p16INK4A have been identified. The tertiary structure of p16INK4A contains four helix-turn-helix motifs linked by three loops. Twelve tumorigenic mutants of p16INK4A have been constructed and analyzed for their structure and activity, and new mutants have been designed rationally. A fragment of 58 residues at the N terminus of cdk4 important for p16INK4A binding has been identified. The importance of this region was further verified by mutational analysis of cdk4. These results and docking experiments have been used to assess possible modes of binding between p16INK4A and cdk4.


  • Organizational Affiliation

    Department of Chemistry, Ohio State University, Columbus 43210, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TUMOR SUPPRESSOR P16INK4A156Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P42771 (Homo sapiens)
Explore P42771 
Go to UniProtKB:  P42771
PHAROS:  P42771
GTEx:  ENSG00000147889 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP42771
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 90 
  • Conformers Submitted: 18 
  • Selection Criteria: CLOSEST TO MEAN STRUCTURE WHICH SHOWS GOOD AGREEMENT WITH THE CONSTRAINTS. NONE OF THE CONSTRAINTS SHOW NOE VIOLATION BIGGER THAN 0.5 A AND DIHEDRAL ANGLE VIOLATION BIGGER THAN 5 DEGREE. 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-08-13
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations, Other