Structural features of human histone acetyltransferase p300 and its complex with p53
作者: Siddhartha BanerjeeArif MTatini RakshitNeeladri S. RoyTapas K. KunduSiddhartha RoyRupa Mukhopadhyay
作者单位: 1Department of Biological Chemistry, Indian Association for the Cultivation of Science, Kolkata 700032, India
2Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, JNCASR, Jakkur, Bangalore 560064, India
3Structural Biology and Bioinformatics Division, CSIR-Indian Institute of Chemical Biology, Kolkata 700032, India
刊名: FEBS Letters, 2012, Vol.586 (21), pp.3793-3798
来源数据库: Elsevier Journal
DOI: 10.1016/j.febslet.2012.09.012
关键词: full-length p300p53protein tertiary structureAFM
英文摘要: Abstract(#br)The protein p300 is a multifunctional transcriptional coactivator that plays pivotal role in several cellular functions. Although structures of several domains have been solved in isolation, the structures of full-length protein (p300 FL) or its complexes with transcription activators are completely unknown. Herein, we applied atomic force microscopy to visualize p300 FL. We found that it is almost prolate ellipsoidal in shape, having several bulges. We further identified the functionally significant N-terminal and C-terminal regions, by applying domain-specific antibodies and found that they are located near one end and centre of the molecule, respectively. Importantly, we have visualized the complex between p300 FL and tumor suppressor protein p53. The relevance of these...
全文获取路径: Elsevier  (合作)
影响因子:3.582 (2012)

  • histone 组蛋白
  • length 距离
  • complex 超群
  • protein 蛋白质
  • tertiary 第三系
  • features 特征
  • human 人的
  • AFM Amplitude-Frequency Modulation
  • structure 构造