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Updated: Nov 11, 2025

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
The myosin II coiled-coil domain atomic structure in its native environment
Hamidreza Rahmani1,2, Wen Ma3, Zhongjun Hu1
1Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380.
The atomic structure of the myosin tail in Lethocerus indicus flight muscle reveals insights into thick filament assembly and function. This study details coiled-coil uncoiling at the head-tail junction and unusual skip region structures.
Area of Science:
- Muscle biology
- Structural biology
- Biophysics
Background:
- Thick filaments are essential for muscle contraction, composed primarily of myosin.
- Understanding myosin tail structure is key to elucidating muscle mechanics.
Purpose of the Study:
- To describe the atomic structure of the complete myosin tail in Lethocerus indicus flight muscle.
- To compare this structure with existing crystal structures of human cardiac myosin tail segments.
Main Methods:
- Analysis of thick filaments isolated from Lethocerus indicus flight muscle.
- Comparison with crystal structures of recombinant human cardiac myosin tail segments.
Main Results:
- Good overall agreement between filament and crystal structures, with notable exceptions in proximal S2 and skip regions 2 and 4.
- Detailed atomic description of asymmetric coiled-coil uncoiling at the myosin head-tail junction.
- Unusual structural accommodations in skip regions 2 and 4, including altered helix radius and unfolding.
Conclusions:
- The atomic model provides insights into myosin tail structure within thick filaments.
- Findings may contribute to understanding thick filament mechanosensing and muscle contraction.
- Highlights structural variations influencing myosin tail assembly and function.
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