Structure of Cocrystals of Tropomyosin and Troponin

The contraction of vertebrate striated muscle is controlled by proteins found in the thin filament. Contraction is initiated when calcium binds to troponin, causing it and tropomyosin to undergo conformational changes. Tropomyosin is an α-helical protein with two chains (284 residues each) arranged as a coiled-coil. These rod-like molecules form cables wound in the grooves of the actin helix. Bound to each tropomyosin molecule is a troponin complex, consisting of three subunits, each with a different architecture and function. Troponin C binds calcium; troponin I binds actin; and troponin T (259 residues) binds one complex to each tropomyosin molecule. The troponin complex has an elongated shape with troponin C and troponin I forming a globular 'head' region and troponin T a long ($\sim$160 A) tail. This study visualizes the interactions between tropomyosin and troponin using X-ray crystallography.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• White, Steven Paul

Contributors dc:contributor

• Phillips, George N., Jr.,

• Chemistry, Biochemistry
• Biophysics, General

Identifier

(UMI)AAI8823287

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70572