Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational Modeling

Abstract excerpt

<title>Abstract</title> <p>The tetrameric tumor suppressor p53 represents a great challenge for 3D-structural analysis due to its high degree of intrinsic disorder (ca. 40%). We aim to shed light on the structural and functional roles of p53’s C-terminal region in full-length, wild-type human p53 tetramer and their importance for DNA binding. For this, we employed complementary techniques of structural mass spect...

Topics

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• Binding Sites
• Computer Simulation
• Models, Chemical
• Molecular Dynamics Simulation
• Protein Conformation
• Proto-Oncogene Proteins c-mdm2
• Structure-Activity Relationship
• Tumor Suppressor Protein p53

Identifiers and source

Literature Corpus work

984a29c8-4efb-5a6a-ba6b-e3e5999da0bf

DOI

10.21203/rs.3.rs-2271015/v1