The binding domain structure of retinoblastoma-binding proteins. |
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| Authors: | J. Figge K. Breese S. Vajda Q. L. Zhu L. Eisele T. T. Andersen R. MacColl T. Friedrich T. F. Smith |
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| Affiliation: | Department of Medicine, Albany Medical College, New York 12208. |
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| Abstract: | The retinoblastoma gene product (Rb), a cellular growth suppressor, complexes with viral and cellular proteins that contain a specific binding domain incorporating three invariant residues: Leu-X-Cys-X-Glu, where X denotes a nonconserved residue. Hydrophobic and electrostatic properties are strongly conserved in this segment even though the nonconserved amino acids vary considerably from one Rb-binding protein to another. In this report, we present a diagnostic computer pattern for a high-affinity Rb-binding domain featuring the three conserved residues as well as the conserved physico-chemical properties. Although the pattern encompasses only 10 residues (with only 4 of these explicitly defined), it exhibits 100% sensitivity and 99.95% specificity in database searches. This implies that a certain pattern of structural and physico-chemical properties encoded by this short sequence is sufficient to govern specific Rb binding. We also present evidence that the secondary structural conformation through this region is important for effective Rb binding. |
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| Keywords: | CD spectroscopy conformational filtering papilloma virus E7 protein peptide conformation protein-protein binding interactions retinoblastoma protein SV40 T antigen |
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