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The backrub motion: how protein backbone shrugs when a sidechain dances
Ian W Davis1, W Bryan Arendall, David C Richardson
1Department of Biochemistry, Duke University, Durham, North Carolina 27710, USA.
Structure (London, England : 1993)
|February 14, 2006
Summary
Protein crystallography reveals a common "backrub" motion, a subtle backbone flexibility. This motion allows significant sidechain changes while maintaining protein structure and hydrogen bonds.
Area of Science:
- Structural Biology
- Protein Dynamics
- Crystallography
Background:
- Proteins exhibit complex dynamics crucial for function.
- Understanding local backbone motion is key to protein plasticity.
Purpose of the Study:
- To identify and characterize subtle local backbone motions in proteins.
- To investigate the coupling between backbone and sidechain conformational changes.
Main Methods:
- Ultra-high-resolution protein crystallography.
- Analysis of alternate conformations in sub-angstrom crystal structures.
- Utilizing the Backrub modeling tool.
Main Results:
- A prevalent 'backrub' motion was identified as a common mode of local backbone plasticity.
- This motion facilitates large, two-state sidechain conformational changes.
- Backrub motions were observed in two-thirds of significant Cbeta shifts and 3% of total residues.
Conclusions:
- The backrub motion is a significant mechanism for protein backbone accommodation.
- It allows for sidechain plasticity while preserving hydrogen bonds and ideal geometry.
- Backrub modeling is effective for crystallographic rebuilding and protein design.