Kozlov G, Trempe J F, Khaleghpour K, Kahvejian A, Ekiel I, Gehring K
Department of Biochemistry, McGill University and Montreal Joint Center for Structural Biology, 3655 Promenade Sir William Osler, Montreal, QC, Canada H3G 1Y6.
Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4409-13. doi: 10.1073/pnas.071024998. Epub 2001 Apr 3.
We have determined the solution structure of the C-terminal quarter of human poly(A)-binding protein (hPABP). The protein fragment contains a protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases. By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use chemical shift perturbation analysis to identify the peptide binding site in PABC and the major elements involved in peptide recognition. From comparative sequence analysis of PABC-binding peptides, we formulate a preliminary PABC consensus sequence and identify human ataxin-2, the protein responsible for type 2 spinocerebellar ataxia (SCA2), as a potential PABC ligand.
我们已经确定了人多聚腺苷酸结合蛋白（hPABP）C末端四分之一区域的溶液结构。该蛋白质片段包含一个蛋白质结构域，即PABC [多聚腺苷酸结合蛋白C末端结构域]，它也与泛素连接酶的HECT家族相关。通过使用源自PABP相互作用蛋白（Paip）1、Paip2和eRF3的肽段，我们表明PABC作为一个肽结合结构域发挥作用。我们使用化学位移扰动分析来确定PABC中的肽结合位点以及参与肽识别的主要元件。通过对PABC结合肽的比较序列分析，我们制定了一个初步的PABC共有序列，并确定人类ataxin-2（负责2型脊髓小脑共济失调（SCA2）的蛋白质）为潜在的PABC配体。
