Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box

Nat Struct Biol. 1997 May;4(5):390-5. doi: 10.1038/nsb0597-390.

Abstract

The pocket region of retinoblastoma tumour suppressor (Rb) is essential for tumour suppressing activity. The Rb pocket is primarily composed of two domains, A and B. We have determined the X-ray crystal structure of domain A (residues 378-562) at 2.3 A resolution. Domain A consists of nine alpha-helices. The overall arrangement of helices in domain A is remarkably similar to the cyclin-box folds found in the crystal structures of cyclin A and TFIIB. This structure, along with domain B which is predicted to be homologous to the cyclin-box, suggests that the Rb pocket is composed of two cyclin-box fold domains. We present the structural/functional features of the Rb pocket, and the potential binding region for cellular or viral proteins within domain A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Cyclins / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Protein Structure, Tertiary
  • Retinoblastoma Protein / chemistry*
  • Transcription Factor TFIIB
  • Transcription Factors / chemistry

Substances

  • Cyclins
  • Retinoblastoma Protein
  • Transcription Factor TFIIB
  • Transcription Factors

Associated data

  • PDB/1AD6
  • PDB/R1AD6SF