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Biomolecular NMR Assignments

, Volume 13, Issue 1, pp 79–83 | Cite as

NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1)

  • Liping YuEmail author
  • Ravi P. Yadav
  • Nikolai O. ArtemyevEmail author
Article

Abstract

Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a photoreceptor-specific chaperone of phosphodiesterase-6, a key effector enzyme in the phototransduction cascade. It contains an N-terminal FK506-binding protein (FKBP) domain and a C-terminal tetratricopeptide repeat (TPR) domain. Mutations in AIPL1, including many missense mutations in both FKBP and TPR domains, have been associated with Leber congenital amaurosis, a severe inherited retinopathy that causes blindness. TPR-domain containing proteins are known to interact with HSP90. However, the structure of AIPL1–TPR domain is presently not determined and little is known about the contribution of the TPR domain to the chaperone function of AIPL1. Here, we report the backbone and sidechain assignments of the TPR domain of AIPL1. These assignments reveal that AIPL1–TPR is an α-helical protein containing seven α-helices connected via short loops. Peak broadening or structural disorder is observed for a cluster of hydrophobic residues of W218, W222 and L223. Therefore, these assignments provide a framework for further structural determination of AIPL1–TPR domain and its interactions with various binding partners for elucidation of the mechanism of TPR contribution to the chaperone function of AIPL1.

Keywords

TPR AIPL1 Chaperone Phosphodiesterase 6 Tetratricopeptide repeat 

Notes

Acknowledgements

This work was supported by the National Institutes of Health (Grant No. EY-10843) to N.O.A and Pediatric Ophthalmology Career Starter Research Grant from the Knights Templar Eye Foundation to R.P.Y.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflicts of interest.

Ethical approval

All of our experiments comply with accepted ethical standards.

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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  1. 1.Department of BiochemistryUniversity of Iowa Carver College of MedicineIowa CityUSA
  2. 2.CCOM NMR Core FacilityUniversity of Iowa Carver College of MedicineIowa CityUSA
  3. 3.Department of Molecular Physiology and BiophysicsUniversity of Iowa Carver College of MedicineIowa CityUSA
  4. 4.Department of Ophthalmology and Visual SciencesUniversity of Iowa Carver College of MedicineIowa CityUSA

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