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

Nature Structural Biology volume 4, pages 390–395 (1997)Cite this article

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 Å resolution. Domain A consists of nine α-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.

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Authors and Affiliations

  1. Structural Biology Center, Korea Institute of Science and Technology, P. 0. Box 131, Cheongryang, Seoul, 130-650, South Korea

    Hye-Yeon Kim & Yunje Cho

  2. Department of Genetic Engineering, Korea University, Seoul, South Korea

    Hye-Yeon Kim

Authors
  1. Hye-Yeon Kim
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  2. Yunje Cho
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Kim, HY., Cho, Y. Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box. Nat Struct Mol Biol 4, 390–395 (1997). https://doi.org/10.1038/nsb0597-390

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