Solving the Structure of the Raptor-CCT complex

Authors

Grant Ludlam, Brigham Young University
Barry Willardson, Brigham Young University

Keywords

raptor-CCT complex, rapamycin cell, mTOR, cell growth

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

The protein Raptor is an essential component of the mechanistic target of rapamycin (mTOR) cell signaling complex 1 (mTORC1) (1). The mTORC1 complex is a master regulator of cell growth, making it a high-priority target in cancer and inflammation research (2). Before Raptor can be assembled into the mTORC1, it is first folded by the chaperone protein cytosolic chaperonin containing TCP1 (CCT). CCT is composed of two rings of 8 different subunits, which together form a barrel shape. CCT substrates are folded in the 85 Å wide folding cavity inside the barrel.

Recommended Citation

Ludlam, Grant and Willardson, Barry (2016) "Solving the Structure of the Raptor-CCT complex," Journal of Undergraduate Research: Vol. 2016: Iss. 1, Article 207.
Available at: https://scholarsarchive.byu.edu/jur/vol2016/iss1/207