ArticleJournal of molecular biology2010
A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli.Acta crystallographica. Section D, Structural biology · 2026Article
- Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states.Protein science : a publication of the Protein Society · 2021Article
- Monothiol and dithiol glutaredoxin-1 fromIUCrJ · 2020Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Exploring the Roles of Proline in Three-Dimensional Domain Swapping from Structure Analysis and Molecular Dynamics Simulations.The protein journal · 2018Article
- Amino-acid composition after loop deletion drives domain swapping.Protein science : a publication of the Protein Society · 2017Article
- Understanding protein domain-swapping using structure-based models of protein folding.Progress in biophysics and molecular biology · 2017Review
- Salt bridge as a gatekeeper against partial unfolding.Protein science : a publication of the Protein Society · 2016Article
- Identification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid Formation.Frontiers in microbiology · 2016Article
- The Landscape of Intertwined Associations in Homooligomeric Proteins.Biophysical journal · 2015Review
- Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain.Chemical biology & drug design · 2012Article
- Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5' GG Sequence for RTPase Activity.Journal of virology · 2012Article
- Functional repertoire, molecular pathways and diseases associated with 3D domain swapping in the human proteome.Journal of clinical bioinformatics · 2012Article
- NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping.PloS one · 2012Article
- Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A.Protein science : a publication of the Protein Society · 2011Article
- 3DSwap: curated knowledgebase of proteins involved in 3D domain swapping.Database : the journal of biological databases and curation · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Domain swapping, the process in which a structural unit is exchanged between monomers to create a dimer containing two subunits of the monomeric fold, is believed to be an important mechanism for oligomerization and the formation of amyloid fibrils. Structural studies have implicated proline as an important residue for domain swapping due to its increased frequency in hinge regions preceding swapped arms. We hypothesized that proline's unique ability to populate both cis and trans peptide bond conformations may allow proline to act as a conformational gatekeeper, regulating interconversion between monomer and domain-swapped dimer forms. The hinge region of RNase A contains a proline at residue 114 that adopts a cis conformation in the monomer and extends to a trans conformation in the C-terminal domain-swapped dimer. Substitution of P114 with residues that strongly prefer a trans peptide bond (Ala, Gly) results in significant population of the C-terminal domain-swapped dimer under near-physiological conditions (pH 8.0, 37 degrees C). This is in stark contrast to dimerization of wild-type RNase A, which requires incubation under extreme conditions such as lyophilization from acetic acid or elevated temperature. In addition, we observe similar results when cis-P114 is mutated to glycine in a homologous RNase, human pancreatic RNase 1. Our results suggest that isomerization at P114 may facilitate population of a partially unfolded intermediate or alternative structure competent for domain swapping and provide support for a more general role for proline isomerization as a conformational gatekeeper in domain swapping and oligomerization.
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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.