1IPG

SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P

1IPG の概要

• エントリーDOI: 10.2210/pdb1ipg/pdb
• 関連するPDBエントリー: 1IP9
• 分子名称: BEM1 PROTEIN (1 entity in total)
• 機能のキーワード: ubiquitin alpha/beta roll, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm, cytoskeleton: P29366
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9519.92

構造登録者

Terasawa, H.,Noda, Y.,Ito, T.,Hatanaka, H.,Ichikawa, S.,Ogura, K.,Sumimoto, H.,Inagaki, F. (登録日: 2001-05-14, 公開日: 2001-08-15, 最終更新日: 2023-12-27)

主引用文献

Terasawa, H.,Noda, Y.,Ito, T.,Hatanaka, H.,Ichikawa, S.,Ogura, K.,Sumimoto, H.,Inagaki, F.
Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.
EMBO J., 20:3947-3956, 2001

PubMed Abstract: PB1 domains are novel protein modules capable of binding to target proteins that contain PC motifs. We report here the NMR structure and ligand-binding site of the PB1 domain of the cell polarity establishment protein, Bem1p. In addition, we identify the topology of the PC motif-containing region of Cdc24p by NMR, another cell polarity establishment protein that interacts with Bem1p. The PC motif-containing region is a structural domain offering a scaffold to the PC motif. The chemical shift perturbation experiment and the mutagenesis study show that the PC motif is a major structural element that binds to the PB1 domain. A structural database search reveals close similarity between the Bem1p PB1 domain and the c-Raf1 Ras-binding domain. However, these domains are functionally distinct from each other.

PubMed: 11483498
DOI: 10.1093/emboj/20.15.3947

実験手法

SOLUTION NMR