Helical fold prediction for the cyclin box

Proteins. 1996 Jan;24(1):1-17. doi: 10.1002/(SICI)1097-0134(199601)24:1<1::AID-PROT1>3.0.CO;2-O.

Abstract

The smooth progression of the eukaryotic cell cycle relies on the periodic activation of members of a family of cell cycle kinases by regulatory proteins called cyclins. Outside of the cell cycle, cyclin homologs play important roles in regulating the assembly of transcription complexes; distant structural relatives of the conserved cyclin core or "box" can also function as general transcription factors (like TFIIB) or survive embedded in the chain of the tumor suppressor, retinoblastoma protein. The present work attempts the prediction of the canonical secondary, supersecondary, and tertiary fold of the minimal cyclin box domain using a combination of techniques that make use of the evolutionary information captured in a multiple alignment of homolog sequences. A tandem set of closely packed, helical modules are predicted to form the cyclin box domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cyclin B*
  • Cyclin B1
  • Cyclins / chemistry*
  • Cyclins / classification
  • Cyclins / metabolism*
  • Models, Molecular*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding*
  • Retinoblastoma Protein / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Software
  • Transcription Factor TFIIB
  • Transcription Factors / chemistry

Substances

  • Cyclin B
  • Cyclin B1
  • Cyclins
  • Retinoblastoma Protein
  • Transcription Factor TFIIB
  • Transcription Factors