Solving the Structure of MB11 Bound Beta-Tubulin
My project seeks to solve the structure of the binding interaction between Mb11 and -tubulin in microtubules. Microtubules are dynamic cytoskeletal polymers essential to life, composed of tubulin subunits, heterodimers of – and -tubulin, which align longitudinally into linear protofilaments and assemble laterally into a cylinder, forming the microtubule. Mb11 is an antibody that has been found to bind specifically to tubulin in the GTP bound conformation. In contrast to GDP bound tubulin, GTP-bound tubulin is straighter and more stable. This difference allows for the specific recognition of the antibody at this site and I will investigate the nature of this conformational specificity. Using electron microscopy, I will obtain sub-nanometer resolution of this binding interaction. Achieving this three-dimensional structure will enable me to hypothesize about the interactions that give specificity for this antibody to GTP-tubulin on an atomic level.
Message to Sponsor
- Major: Molecular and Cell Biology
- Mentor: Eva Nogales, Molecular and Cell Biology