BIOL 200 Lecture Notes - Lecture 11: Structural Alignment, Supersecondary Structure, Protein Tertiary Structure
28 Mar 2013
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Document Summary
The concept of the domain was first proposed in 1973 by wetlaufer after x-ray crystallographic studies of hen lysozyme and papain and by limited proteolysis studies of immunoglobulins. Wetlaufer defined domains as stable units of protein structure that could fold autonomously. In the past domains have been described as units of compact structure,function and evolution,folding. Each definition is valid and will often overlap. Nature often brings several domains together to form multidomain and multifunctional proteins with a vast number of possibilities. In a multidomain protein, each domain may fulfill its own function independently, or in a concerted manner with its neighbours. Domains can either serve as modules for building up large assemblies such as virus particles or muscle fibres, or can provide specific catalytic or binding sites as found in enzymes or regulatory proteins. An appropriate example is pyruvate kinase, a glycolytic enzyme that plays an important role in regulating the flux from fructose-1,6-biphosphate to pyruvate.
