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The π-helix translates structure into function

Published online by Cambridge University Press:  01 January 2000

TODD M. WEAVER
TODD M. WEAVER
Affiliation:
University of Wisconsin La Crosse, Department of Chemistry, La Crosse, Wisconsin 54601
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Abstract

A search for the occurrence of the rare π-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 π-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 π-helices will be addressed in regard to protein function. It is clear upon closer examination that the conformation of the π-helix has evolved to provide unique structural features within a variety of proteins.

Keywords

α-helixπ-helixcatechol-o-methyltransferasefumarase Cglycogen phosphorylaselipoxygenasephotoactive yellow proteinsecondary structureserine carboxypeptidase
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 1 , January 2000 , pp. 201 - 206
Copyright
© 2000 The Protein Society

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