Journal article
NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1)
Biomolecular NMR assignments, Vol.13(1), pp.79-83
04/2019
DOI: 10.1007/s12104-018-9856-x
PMCID: PMC6440825
PMID: 30341566
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.
Details
- Title: Subtitle
- NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1)
- Creators
- Liping Yu - CCOM NMR Core Facility, University of Iowa Carver College of Medicine, Iowa City, IA, 52242, USA. liping-yu@uiowa.eduRavi P Yadav - Department of Molecular Physiology and Biophysics, University of Iowa Carver College of Medicine, 5-532 BSB, 51 Newton Road, Iowa City, IA, 52242, USANikolai O Artemyev - Department of Ophthalmology and Visual Sciences, University of Iowa Carver College of Medicine, Iowa City, IA, 52242, USA. nikolai-artemyev@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Biomolecular NMR assignments, Vol.13(1), pp.79-83
- DOI
- 10.1007/s12104-018-9856-x
- PMID
- 30341566
- PMCID
- PMC6440825
- NLM abbreviation
- Biomol NMR Assign
- ISSN
- 1874-2718
- eISSN
- 1874-270X
- Publisher
- Netherlands
- Grant note
- R01 EY010843 / NEI NIH HHS
- Language
- English
- Date published
- 04/2019
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Biochemistry and Molecular Biology; Medicine Administration; Ophthalmology and Visual Sciences
- Record Identifier
- 9984070611902771
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