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Solution structure of Ca2+-free rat alpha-parvalbumin.

Henzl MT, Tanner JJ
Protein Sci 17 431-8 (2008)
Cited: 13 times
EuropePMC logo PMID: 18218708

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.

Articles - 2jww mentioned but not cited (2)

  1. Solution structure of Ca2+-free rat alpha-parvalbumin. Henzl MT, Tanner JJ. Protein Sci 17 431-438 (2008)
  2. Structural Changes beyond the EF-Hand Contribute to Apparent Calcium Binding Affinities: Insights from Parvalbumins. Immadisetty K, Sun B, Kekenes-Huskey PM. J Phys Chem B 125 6390-6405 (2021)


Reviews citing this publication (4)

  1. Cytosolic Ca2+ buffers. Schwaller B. Cold Spring Harb Perspect Biol 2 a004051 (2010)
  2. Cytosolic Ca2+ Buffers Are Inherently Ca2+ Signal Modulators. Schwaller B. Cold Spring Harb Perspect Biol 12 a035543 (2020)
  3. Designing proteins to combat disease: Cardiac troponin C as an example. Davis JP, Shettigar V, Tikunova SB, Little SC, Liu B, Siddiqui JK, Janssen PM, Ziolo MT, Walton SD. Arch Biochem Biophys 601 4-10 (2016)
  4. What Is Parvalbumin for? Permyakov EA, Uversky VN. Biomolecules 12 656 (2022)

Articles citing this publication (7)

  1. Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs. Kazakov AS, Sokolov AS, Vologzhannikova AA, Permyakova ME, Khorn PA, Ismailov RG, Denessiouk KA, Denesyuk AI, Rastrygina VA, Baksheeva VE, Zernii EY, Zinchenko DV, Glazatov VV, Uversky VN, Mirzabekov TA, Permyakov EA, Permyakov SE. J Biomol Struct Dyn 35 78-91 (2017)
  2. Is high concentration of parvalbumin a requirement for superfast relaxation? Tikunov BA, Rome LC. J Muscle Res Cell Motil 30 57-65 (2009)
  3. Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization. Wafer LN, Tzul FO, Pandharipande PP, Makhatadze GI. Biochemistry 52 5844-5856 (2013)
  4. Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. Schuermann JP, Tan A, Tanner JJ, Henzl MT. J Mol Biol 397 991-1002 (2010)
  5. Solution structures of chicken parvalbumin 3 in the Ca(2+)-free and Ca(2+)-bound states. Henzl MT, Tanner JJ, Tan A. Proteins 79 752-764 (2011)
  6. The Highly Conservative Cysteine of Oncomodulin as a Feasible Redox Sensor. Vologzhannikova AA, Khorn PA, Shevelyova MP, Kazakov AS, Emelyanenko VI, Permyakov EA, Permyakov SE. Biomolecules 11 66 (2021)
  7. Characterization of avian thymic hormone and chicken parvalbumin 3 target cells. Novak Kujundžić R, Steffens WL, Brewer JM, Henzl MT, Ragland WL. Int Immunopharmacol 15 282-288 (2013)


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