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1HN, 13C, and 15N resonance assignments of human calmodulin bound to a peptide derived from the STRA6 vitamin A transporter (CaMBP2)

  • Kristen M. VarneyEmail author
  • Paul T. Wilder
  • Raquel Godoy-Ruiz
  • Filippo Mancia
  • David J. Weber
Article

Abstract

Vitamin A is a necessary nutrient for all mammals, and it is required for the transcription of many genes and vital for vision. While fasting, the vitamin A alcohol form (Retinol) from storage in the liver is mobilized and transported through the bloodstream while bound to retinol binding protein (RBP). Details of how exactly vitamin A is released from RBP and taken into the cells are still unclear. As part of the effort to elucidate the specifics of this process, single-particle cryo-electron microscopy structural studies of STRA6 (the RBP receptor 75-kDa transmembrane receptor protein) were recently reported by Chen et al. (Science,  https://doi.org/10.1126/science.aad8266, 2016). Interestingly, STRA6 from zebrafish was shown to be a stable dimer and bound to calmodulin (CaM), forming a 180-kDa complex. The topology of the STRA6 complex includes 18 transmembrane helices (nine per protomer) and two long horizontal intramembrane helices interacting at the dimer core (Chen et al., in Science,  https://doi.org/10.1126/science.aad8266, 2016). CaM was shown to interact with three regions of STRA6, termed CaMBP1, CaMBP2, and CaMBP3, with the most extensive interactions involving CaMBP2. To further our understanding of Ca2+-dependence of CaM-STRA6 complex formation, studies of the structure and dynamic properties of the CaMBP2–CaM complex were initiated. For this, the 1HN, 13C, and 15N backbone resonance assignments of the 148 amino acid Ca2+-bound calmodulin protein bound to the 27-residue CaMBP2 peptide derived from STRA6 were completed here using heteronuclear multidimensional NMR spectroscopy.

Keywords

Vitamin A Retinoic acid Calmodulin STRA6 

Notes

Acknowledgements

This work is supported by 1R01EY027405 (F.M.) and shared instrumentation grants to the UMB NMR center from the National Institutes of Health [S10 RR10441, S10 RR15741, S10 RR16812, and S10 RR23447 (D.J.W.)] and from the National Science Foundation (DBI 1005795 to D.J.W.). This work was also supported via the Center for Biomolecular Therapeutics (CBT) at the University of Maryland.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT)University of Maryland School of MedicineBaltimoreUSA
  2. 2.Department of Physiology and Cellular BiophysicsColumbia UniversityNew YorkUSA

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