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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
Published on: November 5, 2018
Solution structure of human von Willebrand factor studied using small angle neutron scattering
Indrajeet Singh1, Harish Shankaran, Mark E Beauharnois
1Department of Chemical and Biological Engineering, State University of New York, Buffalo, NY 14260, USA.
The Journal of Biological Chemistry
|October 21, 2006
Summary
The solution structure of von Willebrand factor (VWF) was studied using scattering techniques. VWF multimers are loosely packed ellipsoids, and local structural changes, not large-scale ones, trigger proteolysis.
Area of Science:
- Biophysics
- Structural Biology
- Hematology
Background:
- Atherothrombosis involves von Willebrand factor (VWF) binding to platelets under high shear stress.
- Understanding VWF's solution structure is crucial for comprehending its role in thrombosis.
Purpose of the Study:
- To elucidate the solution structure of human VWF multimers and protomers.
- To investigate the structural basis of VWF's interaction with platelets and its proteolysis.
Main Methods:
- Light and small-angle neutron scattering were employed to determine VWF structure.
- Biochemical methods including cross-linking and Western blotting were used to study intermonomer interactions.
Main Results:
- VWF multimers and protomers resemble prolate ellipsoids with distinct dimensions (e.g., 175 x 28 nm for multimers).
- Substructural domains within VWF multimers reflect protomer quaternary structure and individual functional domains.
- Local structural changes (<10 nm) upon chemical treatment affect VWF proteolysis susceptibility without altering overall dimensions.
- Stable non-covalent interactions stabilize the multimeric VWF structure.
Conclusions:
- Multimeric VWF is a loosely packed ellipsoidal protein stabilized by non-covalent intermonomer interactions.
- Local conformational changes are sufficient to enable ADAMTS-13-mediated proteolysis, a key step in regulating atherothrombosis.
