1ipg
From Proteopedia
SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P
Structural highlights
FunctionBEM1_YEAST Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.[1] 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 PubMedPB1 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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