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首页> 美国政府科技报告 >Structural Studies of the pRB Tumor Suppressor Complexed with Human Papillomavirus E7 Proteins
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Structural Studies of the pRB Tumor Suppressor Complexed with Human Papillomavirus E7 Proteins

机译：与人乳头瘤病毒E7蛋白复合的pRB肿瘤抑制因子的结构研究

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Since viral oncoproteins are expected to compete with and imitate interactions that pRB has with cyclin Dl, understanding high affinity pRB-viral oncoprotein complexes will provide tremendous insight into the specific interactions required for the development of small compounds that can destabilize pRB-cyclin Dl complexes in cyclin Dl -mediated breast cancer. Therefore, the primary goal of this project is to determine the three dimensional structure of pRB bound HPV E7 and Adenovirus 5 El A. Additionally, since p53 functions as a tumor suppressor that is often inactivated in breast cancer, a secondary goal of this project is to determine the structure of the PCAF acetyltransferase domain with coenzyme A and a p53-derived peptide in order to gain insight into PCAF-mediated p53 activation This study demonstrates that bacterially coexpressed pRB(376-792) and viral oncoproteins form complexes. To date, these purified complexes have resisted crystallization. However, crystallography of HPV 1 a E7 and NMR studies of Adenovirus 5 El A have had preliminary success. Sedimentation equilibrium experiments of the pRB/viral oncoprotein complexes and their individual components have been utilized to characterize protein oligomerization states. Additionally, the crystal structure of PCAF bound to coenzyme A has been solved and provides insight into PCAF- mediated p53 acetylation and activation.

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