ArticleProtein science : a publication of the Protein Society2007
Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin).
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 36 citations in OpenAlex.
- Calcium-binding proteins as allergens.Frontiers in allergy · 2026Review
- Calcium dissociation with carbonate ions from Pf-SCP, sarcoplasmic calcium-binding protein in Pinctada fucata, contributes to calcium mineralization for shell formation.Protein science : a publication of the Protein Society · 2025Article
- Oncomodulin (OCM) uniquely regulates calcium signaling in neonatal cochlear outer hair cells.Cell calcium · 2022Article
- What Is Parvalbumin for?Biomolecules · 2022Review
- The Highly Conservative Cysteine of Oncomodulin as a Feasible Redox Sensor.Biomolecules · 2021Article
- Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cytosolic CaCold Spring Harbor perspectives in biology · 2020Review
- Oncomodulin: The Enigmatic Parvalbumin Protein.Frontiers in molecular neuroscience · 2019Article
- Understanding Ion Binding Affinity and Selectivity in β-Parvalbumin Using Molecular Dynamics and Mean Spherical Approximation Theory.The journal of physical chemistry. B · 2016Article
- Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization.Biochemistry · 2013Article
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Ca(2+) sensor proteins in dendritic spines: a race for Ca(2+).Frontiers in molecular neuroscience · 2012Article
- Cytosolic Ca2+ buffers.Cold Spring Harbor perspectives in biology · 2010Review
- Oncomodulin identifies different hair cell types in the mammalian inner ear.The Journal of comparative neurology · 2010Article
- Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states.Journal of molecular biology · 2010Article
- Is high concentration of parvalbumin a requirement for superfast relaxation?Journal of muscle research and cell motility · 2009Article
- Solution structure of Ca2+-free rat alpha-parvalbumin.Protein science : a publication of the Protein Society · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Relative to other parvalbumin isoforms, the mammalian beta-parvalbumin (oncomodulin) displays attenuated divalent ion affinity. High-resolution structural data for the Ca(2+)-bound protein have provided little insight into the physical basis for this behavior, prompting an examination of the unliganded state. This article describes the solution structure and peptide backbone dynamics of Ca(2+)-free rat beta-parvalbumin (beta-PV). Ca(2+) removal evidently provokes significant structural alterations. Interaction between the D helix and the AB domain in the Ca(2+)-bound protein is greatly diminished in the apo-form, permitting the D helix to straighten. There is also a significant reorganization of the hydrophobic core and a concomitant remodeling of the interface between the AB and CD-EF domains. These modifications perturb the orientation of the C and D helices, and the energetic penalty associated with their reversal could contribute to the low-affinity signature of the CD site. By contrast, Ca(2+) removal causes a comparatively minor perturbation of the E and F helices, consistent with the more typical divalent ion affinity observed for the EF site. Ca(2+)-free rat beta-PV retains structural rigidity on the picosecond-nanosecond timescale. At 20 degrees C, the majority of amide vectors show no evidence for motion on timescales above 20 ps, and the average order parameter for the entire molecule is 0.92.
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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.