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Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.

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.

SUBMITTER: Terasawa H 

PROVIDER: S-EPMC149143 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature

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Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.

Terasawa H H   Noda Y Y   Ito T T   Hatanaka H H   Ichikawa S S   Ogura K K   Sumimoto H H   Inagaki F F  

The EMBO journal 20010801 15

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 per  ...[more]