Structural Insights into the Folding Defects of Oncogenic pVHL Lead to Correction of Its Function In Vitro

Loss of function mutations in the von Hippel-Lindau (pVHL) tumor suppressor protein are tumorigenic. In silico analysis of the structure and folding of WT pVHL identified in its core an aromatic tetrahedron, essential for stabilizing the protein. The mutations disrupt the aromatic tetrahedron, leadi...

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Bibliographic Details
Published in:	PloS one 2013-06, Vol.8 (6), p.e66333
Main Authors:	Shmueli, Merav D., Schnaider, Lee, Rosenblum, Daniel, Herzog, Gal, Gazit, Ehud, Segal, Daniel
Format:	Article
Language:	English
Subjects:	Analysis Apoptosis Arginine Arginine - chemistry Bacteria Biology Biotechnology Cancer Carcinoma, Renal Cell - genetics Defects Escherichia coli Folding Humans Hypoxia-Inducible Factor 1, alpha Subunit - chemistry Kidney Neoplasms - genetics Kinases Life sciences Models, Molecular Molecular Weight Mutation Mutation, Missense Neoplasia Osmolar Concentration Peptide Fragments - chemistry Protein Binding Protein Folding Protein Structure, Tertiary Proteins Proteomics Restoration Trends Tumor suppressor genes Tumors VHL protein Von Hippel-Lindau Tumor Suppressor Protein - chemistry Von Hippel-Lindau Tumor Suppressor Protein - genetics
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