[HTML][HTML] Structural insights into the folding defects of oncogenic pVHL lead to correction of its function in vitro
MD Shmueli, L Schnaider, D Rosenblum, G Herzog… - PloS one, 2013 - journals.plos.org
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, leading to misfolding of pVHL. Using biophysical methods we confirmed the in
silico predictions, demonstrating that mutant pVHL proteins have lower stability than the WT,
distort the core domain and as a result reduce the ability of the protein to bind its target HIF …
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, leading to misfolding of pVHL. Using biophysical methods we confirmed the in
silico predictions, demonstrating that mutant pVHL proteins have lower stability than the WT,
distort the core domain and as a result reduce the ability of the protein to bind its target HIF …
[PDF][PDF] Structural Insights into the Folding Defects of Oncogenic pVHL Lead to
MD Shmueli, L Schnaider, D Rosenblum, G Herzog… - 2013 - academia.edu
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, leading to misfolding of pVHL. Using biophysical methods we confirmed the in
silico predictions, demonstrating that mutant pVHL proteins have lower stability than the WT,
distort the core domain and as a result reduce the ability of the protein to bind its target HIF …
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, leading to misfolding of pVHL. Using biophysical methods we confirmed the in
silico predictions, demonstrating that mutant pVHL proteins have lower stability than the WT,
distort the core domain and as a result reduce the ability of the protein to bind its target HIF …
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