High-resolution structure of the oligomerization domain of p53 by multidimensional NMR
Science, 1994•science.org
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the
tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic
resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with
a topology made up from a dimer of dimers. The two primary dimers each comprise two
antiparallel helices linked by an antiparallel β sheet. One β strand and one helix are
contributed from each monomer. The interface between the two dimers forming the tetramer …
tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic
resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with
a topology made up from a dimer of dimers. The two primary dimers each comprise two
antiparallel helices linked by an antiparallel β sheet. One β strand and one helix are
contributed from each monomer. The interface between the two dimers forming the tetramer …
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel β sheet. One β strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel β sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.
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