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Refinement of recombinant oncomodulin at 1.30 A resolution
F R Ahmed1, D R Rose, S V Evans
1Institute for Biological Sciences, National Research Council of Canada, Ottawa.
Journal of Molecular Biology
|April 20, 1993
Summary
This study refined the oncomodulin crystal structure, revealing molecular aggregation via calcium ions and an unstable CD loop. These features may explain oncomodulin
Area of Science:
- Structural Biology
- Biochemistry
- X-ray Crystallography
Background:
- Oncomodulin is a calcium-binding protein with unique biological functions.
- Previous structural data lacked high resolution for definitive molecular insights.
Purpose of the Study:
- To refine the crystal structure of recombinant oncomodulin at high resolution (1.30 Å).
- To elucidate the molecular basis for oncomodulin's biological peculiarities.
Main Methods:
- X-ray diffraction data collection from recombinant oncomodulin.
- Restrained least-squares refinement of the crystal structure.
- Analysis of electron density maps and molecular model.
Main Results:
- A high-resolution (1.30 Å) crystal structure of oncomodulin was determined.
- The structure reveals molecular aggregation mediated by intermolecular calcium ions, similar to native oncomodulin.
- An unstable CD loop due to an Asp59 substitution and disordered surface residues were identified.
Conclusions:
- The refined structure provides definitive insights into oncomodulin's molecular organization.
- Intermolecular calcium-mediated aggregation and CD loop instability are key features potentially explaining oncomodulin's biological distinctiveness.