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Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif
Author(s) -
Terasawa Hiroaki,
Noda Yukiko,
Ito Takashi,
Hatanaka Hideki,
Ichikawa Saori,
Ogura Kenji,
Sumimoto Hideki,
Inagaki Fuyuhiko
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.15.3947
Subject(s) - biology , motif (music) , plasma protein binding , computational biology , microbiology and biotechnology , acoustics , physics
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.