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The π‐helix translates structure into function
Author(s) -
Weaver Todd M.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.1.201
Subject(s) - helix (gastropod) , protein structure , alpha helix , crystallography , protein data bank , chemistry , biology , biochemistry , ecology , snail
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.

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