Kim, HY Cho, Y 2024-01-21T18:32:10Z 2024-01-21T18:32:10Z 2021-09-05 1997-05 1072-8368 https://pubs.kist.re.kr/handle/201004/143827 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 Angstrom 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. English NATURE PUBLISHING GROUP GENE-PRODUCT RB GENE CRYSTAL-STRUCTURE PROTEIN PROGRAM DOMAIN TFIIB COMPLEX BINDING RECOGNITION Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box Article 10.1038/nsb0597-390 1 NATURE STRUCTURAL BIOLOGY, v.4, no.5, pp.390 - 395 NATURE STRUCTURAL BIOLOGY 4 5 390 395 scie scopus A1997WX02800015 2-s2.0-0030996584 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article GENE-PRODUCT RB GENE CRYSTAL-STRUCTURE PROTEIN PROGRAM DOMAIN TFIIB COMPLEX BINDING RECOGNITION tumour suppressor