1ip9 | pdb_00001ip9

SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P

spinqualitylabelsall models 1ip9, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ip9 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ipg Resources: FirstGlance, OCA, RCSB, PDBsum Function [BEM1_YEAST] Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif.,Terasawa H, Noda Y, Ito T, Hatanaka H, Ichikawa S, Ogura K, Sumimoto H, Inagaki F EMBO J. 2001 Aug 1;20(15):3947-56. PMID:11483498 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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