Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies
2007
How Antibodies Change Shape to Bind Different Antigens
publication
Evidence: moderate
Author Information
Author(s): Keskin Ozlem
Primary Institution: Koc University, Center for Computational Biology and Bioinformatics
Hypothesis
The native state of an antibody is not defined by a single rigid conformation but instead with an ensemble of similar conformations that co-exist at equilibrium.
Conclusion
The study suggests that antibodies can bind to different antigens due to their intrinsic conformational flexibility.
Supporting Evidence
- The intrinsic fluctuations of antibodies allow them to recognize a wide variety of antigens.
- The study found that the pre-existing equilibrium model explains how antibodies can bind to multiple antigens.
- Experimental data supports the idea that antibodies exist in multiple conformations even when unbound.
Takeaway
Antibodies can change their shape to fit different germs, kind of like how a stretchy glove can fit different hands.
Methodology
An elastic network model (Anisotropic Network Model) was used to study the intrinsic fluctuations of antibodies and other proteins.
Digital Object Identifier (DOI)
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