ArticlePloS one2012
Tolerance of protein folding to a circular permutation in a PDZ domain.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Circular permutation at azurin's active site slows down its folding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- The Conformational Plasticity Vista of PDZ Domains.Life (Basel, Switzerland) · 2020Review
- Specificity in PDZ-peptide interaction networks: Computational analysis and review.Journal of structural biology: X · 2020Review
- Structural Determinants of Misfolding in Multidomain Proteins.PLoS computational biology · 2016Article
- Article
- The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.Journal of molecular biology · 2015Article
- Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus.Scientific reports · 2015Article
- Network analysis of circular permutations in multidomain proteins reveals functional linkages for uncharacterized proteins.Cancer informatics · 2014Article
- Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.Scientific reports · 2013Article
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Authors and funding
8 authors.
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Abstract
Circular permutation is a common molecular mechanism for evolution of proteins. However, such re-arrangement of secondary structure connectivity may interfere with the folding mechanism causing accumulation of folding intermediates, which in turn can lead to misfolding. We solved the crystal structure and investigated the folding pathway of a circularly permuted variant of a PDZ domain, SAP97 PDZ2. Our data illustrate how well circular permutation may work as a mechanism for molecular evolution. The circular permutant retains the overall structure and function of the native protein domain. Further, unlike most examples in the literature, this circular permutant displays a folding mechanism that is virtually identical to that of the wild type. This observation contrasts with previous data on the circularly permuted PDZ2 domain from PTP-BL, for which the folding pathway was remarkably affected by the same mutation in sequence connectivity. The different effects of this circular permutation in two homologous proteins show the strong influence of sequence as compared to topology. Circular permutation, when peripheral to the major folding nucleus, may have little effect on folding pathways and could explain why, despite the dramatic change in primary structure, it is frequently tolerated by different protein folds.
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