1G9L

SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN

1G9L の概要

• エントリーDOI: 10.2210/pdb1g9l/pdb
• NMR情報: BMRB: 4915
• 分子名称: POLYADENYLATE-BINDING PROTEIN 1 (1 entity in total)
• 機能のキーワード: all-helical domain, rna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15286.45

構造登録者

Kozlov, G.,Trempe, J.-F.,Khaleghpour, K.,Kahvejian, A.,Ekiel, I.,Gehring, K. (登録日: 2000-11-24, 公開日: 2001-03-14, 最終更新日: 2024-05-22)

主引用文献

Kozlov, G.,Trempe, J.F.,Khaleghpour, K.,Kahvejian, A.,Ekiel, I.,Gehring, K.
Structure and function of the C-terminal PABC domain of human poly(A)-binding protein.
Proc.Natl.Acad.Sci.USA, 98:4409-4413, 2001

PubMed Abstract: 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.

PubMed: 11287632
DOI: 10.1073/pnas.071024998

実験手法

SOLUTION NMR