title: The pi-helix translates structure into function.
abstract: A search for the occurrence of the rare pi-helix was performed with Iditis from the Oxford Molecular Group upon the Protein Data Bank. In 8 of the 10 confirmed crystal structures that harbor the pi-helix, its unique conformation has been linked directly to the formation or stabilization of a specific binding site within the protein. In the discussion to follow, the role for each of these eight pi-helices will be addressed in regard to protein function. It is clear upon closer examination that the conformation of the pi-helix has evolved to provide unique structural features within a variety of proteins.
authors.affiliation: University of Wisconsin La Crosse, Department of Chemistry, 54601, USA. weaver@mail.uwlax.edu
authors.forename: T M
authors.initials: TM
authors.lastname: Weaver
mesh_terms: D018360:Crystallography, X-Ray; D005649:Fumarate Hydratase / Q000737:chemistry; D008084:Lipoxygenase / Q000737:chemistry; D008958:Models, Molecular; D006005:Phosphorylases / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: D008084:Lipoxygenase; D006005:Phosphorylases; C095842:fumarase C; D005649:Fumarate Hydratase