ArticleOpen biology2021
Metamorphic proteins: the Janus proteins of structural biology.
Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Janus kinase inhibitors in atopic dermatitis: an umbrella review of meta-analyses.Frontiers in immunology · 2024Pooled it
- Embrace Disorder as a Function: Bio-Informed Biomaterials Design Advanced by Intrinsically Disordered Proteins.Biomimetics (Basel, Switzerland) · 2026Article
- Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026Article
- Article
- Structure-guided design of a synthetic bile acid that inhibits Clostridioides difficile TcdB toxin.Nature microbiology · 2025Article
- Morpheus: a fragment-based algorithm to predict fold-switching behaviour in proteins across proteomes.Bioinformatics (Oxford, England) · 2025Article
- Efficient protein structure generation with sparse denoising models.Nature machine intelligence · 2025Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Aromatic-aromatic interactions drive fold switch of GA95 and GB95 with three residue difference.Chemical science · 2025Article
- Viral Receptor-Binding Protein Evolves New Function through Mutations That Cause Trimer Instability and Functional Heterogeneity.Molecular biology and evolution · 2024Article
- Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023Review
- Proteome-Wide Structural Computations Provide Insights into Empirical Amino Acid Substitution Matrices.International journal of molecular sciences · 2023Article
- Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022Review
- Dimer dissociation is a key energetic event in the fold-switch pathway of KaiB.Biophysical journal · 2022Article
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Authors and funding
3 authors.
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Abstract
The structural paradigm that the sequence of a protein encodes for a unique three-dimensional native fold does not acknowledge the intrinsic plasticity encapsulated in conformational free energy landscapes. Metamorphic proteins are a recently discovered class of biomolecules that illustrate this plasticity by folding into at least two distinct native state structures of comparable stability in the absence of ligands or cofactors to facilitate fold-switching. The expanding list of metamorphic proteins clearly shows that these proteins are not mere aberrations in protein evolution, but may have actually been a consequence of distinctive patterns in selection pressure such as those found in virus-host co-evolution. In this review, we describe the structure-function relationships observed in well-studied metamorphic protein systems, with specific focus on how functional residues are sequestered or exposed in the two folds of the protein. We also discuss the implications of metamorphosis for protein evolution and the efforts that are underway to predict metamorphic systems from sequence properties alone.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.