S
Svetlana Gorina
Researcher at Memorial Sloan Kettering Cancer Center
Publications - 4
Citations - 5663
Svetlana Gorina is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Protein structure & Binding site. The author has an hindex of 4, co-authored 4 publications receiving 5386 citations.
Papers
More filters
Journal ArticleDOI
Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
TL;DR: The crystal structure of a complex containing the core domain of human p53 and a DNA binding site provides a framework for understanding how mutations inactivate it, and supports the hypothesis that DNA binding is critical for the biological activity of p53.
Journal ArticleDOI
Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain.
Paul H. Kussie,Svetlana Gorina,Vincent Marechal,Brian Elenbaas,Jacque Moreau,Arnold J. Levine,Nikola P. Pavletich +6 more
TL;DR: The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-Residue transactivation domain peptide of p53 revealed that MDM 2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic α helix, supporting the hypothesis thatMDM2 inactivates p53 by concealing its transactivationdomain.
Journal ArticleDOI
Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.
TL;DR: The crystal structure of the p53 core domain bound to the 53BP2 protein revealed that the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and provides evidence that the 53 BP2-p53 complex forms in vivo and may have a critical role in the p 53 pathway of tumor suppression.
Journal ArticleDOI
Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms
TL;DR: The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent.