Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
نویسندگان
چکیده
منابع مشابه
The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
The 14-3-3 family of proteins mediates signal transduction by binding to phosphoserine-containing proteins. Using phosphoserine-oriented peptide libraries to probe all mammalian and yeast 14-3-3s, we identified two different binding motifs, RSXpSXP and RXY/FXpSXP, present in nearly all known 14-3-3 binding proteins. The crystal structure of 14-3-3zeta complexed with the phosphoserine motif in p...
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The 14-3-3 family of phosphoserine/threonine-recognition proteins engage multiple nodes in signaling networks that control diverse physiological and pathophysiological functions and have emerged as promising therapeutic targets for such diseases as cancer and neurodegenerative disorders. Thus, small molecule modulators of 14-3-3 are much needed agents for chemical biology investigations and the...
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Transit sequences of chloroplast-destined precursor proteins are phosphorylated on a serine or threonine residue. The amino acid motif around the phosphorylation site is related to the phosphopeptide binding motif for 14-3-3 proteins. Plant 14-3-3 proteins interact specifically with wheat germ lysate-synthesized chloroplast precursor proteins and require an intact phosphorylation motif within t...
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Let G be a (p, q) graph. Let f : V (G) → {1, 2, . . . , k} be a map. For each edge uv, assign the label gcd (f(u), f(v)). f is called k-prime cordial labeling of G if |vf (i) − vf (j)| ≤ 1, i, j ∈ {1, 2, . . . , k} and |ef (0) − ef (1)| ≤ 1 where vf (x) denotes the number of vertices labeled with x, ef (1) and ef (0) respectively denote the number of edges labeled with 1 and not labeled with 1....
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2003
ISSN: 0261-4189,1460-2075
DOI: 10.1093/emboj/cdg104