ArticleProtein science : a publication of the Protein Society2008
Solution structure of Ca2+-free rat alpha-parvalbumin.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- What Is Parvalbumin for?Biomolecules · 2022Review
- Structural Changes beyond the EF-Hand Contribute to Apparent Calcium Binding Affinities: Insights from Parvalbumins.The journal of physical chemistry. B · 2021Article
- The Highly Conservative Cysteine of Oncomodulin as a Feasible Redox Sensor.Biomolecules · 2021Article
- Cytosolic CaCold Spring Harbor perspectives in biology · 2020Review
- Structural implications of CaScientific reports · 2016Article
- Designing proteins to combat disease: Cardiac troponin C as an example.Archives of biochemistry and biophysics · 2016Review
- Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization.Biochemistry · 2013Article
- Cytosolic Ca2+ buffers.Cold Spring Harbor perspectives in biology · 2010Review
- 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
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammals express two parvalbumins-an alpha isoform and a beta isoform. In rat, the alpha-parvalbumin (alpha-PV) exhibits superior divalent ion affinity. For example, the standard free energies for Ca2+ binding differ by 5.5 kcal/mol in 0.15 M KCl (pH 7.4). High-resolution structures of the Ca2+-bound proteins provide little insight into this disparity, prompting a structural analysis of the apo-proteins. A recent analysis of rat beta-PV suggested that Ca2+ removal provokes substantial conformational changes-reorientation of the C, D, and E helices; reorganization of the hydrophobic core; reduced interdomain contact; and remodeling of the AB domain. The energetic penalty attendant to reversing these changes, it was suggested, could contribute to the attenuated divalent ion-binding signature of that protein. That hypothesis is supported by data presented herein, describing the solution structure and peptide backbone dynamics of Ca2+-free rat alpha-PV. In marked contrast to rat beta-PV, the apo- and Ca2+-loaded forms of the rat alpha isoform are quite similar. Significant structural differences appear to be confined to the loop regions of the molecule. This finding implies that the alpha-PV isoform enjoys elevated divalent ion affinity because the metal ion-binding events do not require major structural rearrangement and the concomitant sacrifice of binding energy.
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