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The origami of thioredoxin‐like folds
Author(s) -
Pan Jonathan L.,
Bardwell James C.A.
Publication year - 2006
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.062268106
Subject(s) - superfamily , thioredoxin , protein folding , ingenuity , computational biology , structural motif , biology , protein family , conserved sequence , protein structure , motif (music) , genetics , microbiology and biotechnology , biochemistry , peptide sequence , physics , gene , neoclassical economics , economics , acoustics
Origami is the Japanese art of folding a piece of paper into complex shapes and forms. Much like origami of paper, Nature has used conserved protein folds to engineer proteins for a particular task. An example of a protein family, which has been used by Nature numerous times, is the thioredoxin superfamily. Proteins in the thioredoxin superfamily are all structured with a β‐sheet core surrounded with α‐helices, and most contain a canonical CXXC motif. The remarkable feature of these proteins is that the link between them is the fold; however, their reactivity is different for each member due to small variations in this general fold as well as their active site. This review attempts to unravel the minute differences within this protein family, and it also demonstrates the ingenuity of Nature to use a conserved fold to generate a diverse collection of proteins to perform a number of different biochemical tasks.