ArticleBiochemistry2008
The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- Sequence-based prediction of condensate composition reveals that specificity can emerge from multivalent interactions among disordered regions.Communications chemistry · 2025Article
- Sequence-based prediction of condensate composition reveals that specificity can emerge from multivalent interactions among disordered regions.bioRxiv : the preprint server for biology · 2025Article
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.Communications biology · 2022Article
- Investigating Intrinsically Disordered Proteins With Brownian Dynamics.Frontiers in molecular biosciences · 2022Article
- Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins.The Journal of biological chemistry · 2021Article
- Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability.International journal of molecular sciences · 2021Review
- The Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2): Biochemical and Biophysical Properties, and Its Association with Adipogenesis.International journal of molecular sciences · 2020Review
- Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Production of Intrinsically Disordered Proteins for Biophysical Studies: Tips and Tricks.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.Cellular and molecular life sciences : CMLS · 2017Review
- Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Proteins · 2017Article
- Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme.FEBS letters · 2016Article
- Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.Journal of chemical theory and computation · 2015Article
- The Dimerization State of the Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2).PloS one · 2015Article
- Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.Nucleic acids research · 2014Article
- Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Proteins · 2014Article
- Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes.Science (New York, N.Y.) · 2014Article
- Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.PLoS computational biology · 2013Article
- The neuroendocrine protein 7B2 is intrinsically disordered.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Sml1 is a small ribonucleotide reductase (RNR) regulatory protein in Saccharomyces cerevisiae that binds to and inhibits RNR activation. NMR studies of 15N-labeled Sml1 (104 residues), as well as of a truncated variant (residues 50-104), have allowed characterization of their molecular properties. Sml1 belongs to the class of intrinsically disordered proteins with a high degree of dynamics and very little stable structure. Earlier suggestions for a dimeric structure of Sml1 were confirmed, and from translation diffusion NMR measurements, a dimerization dissociation constant of 0.1 mM at 4 degreesC could be determined. The hydrodynamic radius for the monomeric form of Sml1 was determined to be 23.4 A, corresponding to a protein size between those of a globular protein and a coil. Formation of a dimer results in a hydrodynamic radius of 34.4 A. The observed chemical shifts showed in agreement with previous studies two segments with transient helical structure, residues 4-20 and 60-86, and relaxation studies clearly showed restricted motion in these segments. A spin-label attached to C14 showed long-range interactions with residues 60-70 and 85-95, suggesting that the N-terminal domain folds onto the C-terminal domain. Importantly, protease degradation studies combined with mass spectrometry indicated that the N-terminal domain is degraded before the C-terminal region and thus may serve as a protection against proteolysis of the functionally important C-terminal region. Dimer formation was not associated with significant induction of structure but was found to provide further protection against proteolysis. We propose that this molecular shielding and protection of vital functional structures from degradation by functionally unimportant sites may be a general attribute of other natively disordered proteins.
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