Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box.
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.
Kim
H Y
HY
Structural Biology Center, Korea Institute of Science and Technology, Cheongryang, Seoul, South Korea.
Cho
Y
Y
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D016213:Cyclins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016160:Retinoblastoma Protein / Q000737:chemistry*; D035581:Transcription Factor TFIIB; D014157:Transcription Factors / Q000737:chemistry
D016213:Cyclins; D016160:Retinoblastoma Protein; D035581:Transcription Factor TFIIB; D014157:Transcription Factors