1IPG
SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P
Summary for 1IPG
| Entry DOI | 10.2210/pdb1ipg/pdb |
| Related | 1IP9 |
| Descriptor | BEM1 PROTEIN (1 entity in total) |
| Functional Keywords | ubiquitin alpha/beta roll, signaling protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm, cytoskeleton: P29366 |
| Total number of polymer chains | 1 |
| Total formula weight | 9519.92 |
| Authors | Terasawa, H.,Noda, Y.,Ito, T.,Hatanaka, H.,Ichikawa, S.,Ogura, K.,Sumimoto, H.,Inagaki, F. (deposition date: 2001-05-14, release date: 2001-08-15, Last modification date: 2023-12-27) |
| Primary citation | 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 Cited by 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: 11483498DOI: 10.1093/emboj/20.15.3947 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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