NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand

Liping Yu; Ravi P Yadav; Nikolai O Artemyev

doi:10.1007/s12104-017-9730-2

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NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand

Journal article

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NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand

Liping Yu, Ravi P Yadav and Nikolai O Artemyev

Biomolecular NMR assignments, Vol.11(1), pp.111-115

04/2017

DOI: 10.1007/s12104-017-9730-2

PMCID: PMC5385707

PMID: 28236226

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https://www.ncbi.nlm.nih.gov/pmc/articles/5385707View

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Abstract

Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a specialized chaperone of phosphodiesterase 6, a key effector enzyme in the phototransduction cascade. The FKBP domain of AIPL1 is known to bind the farnesyl moiety of PDE6. Mutations in AIPL1, including many missense mutations in the FKBP domain, have been associated with Leber congenital amaurosis, a severe blinding disease. Here, we report the backbone and sidechain assignments of the N-terminal FKBP (with a loop deletion) of AIPL1 in complex with a farnesyl ligand. We also compare the predicted secondary structures of FKBP with those of a highly homologous AIP FKBP. These results show that the FKBP domains of AIP and AIPL1 have similar folds, but display subtle differences in structure and dynamics. Therefore, these assignments provide a framework for further elucidation of the mechanism of farnesyl binding and the function of AIPL1 FKBP.

Ligands

Cyclic Nucleotide Phosphodiesterases, Type 6 - metabolism

Sesquiterpenes - metabolism

Intracellular Signaling Peptides and Proteins - chemistry

Humans

Nuclear Magnetic Resonance, Biomolecular

Protein Domains

Intracellular Signaling Peptides and Proteins - metabolism

Details

Title: Subtitle: NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand
Creators: Liping Yu - NMR Core Facility, Carver College of Medicine, University of Iowa, 285 Newton Road, Iowa City, IA, 52242, USA. liping-yu@uiowa.edu
Ravi P Yadav - Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, 51 Newton Road, Iowa City, IA, 52242, USA
Nikolai O Artemyev - Ophthalmology and Visual Sciences, Carver College of Medicine, University of Iowa, Iowa City, IA, 52242, USA. nikolai-artemyev@uiowa.edu
Resource Type: Journal article
Publication Details: Biomolecular NMR assignments, Vol.11(1), pp.111-115
DOI: 10.1007/s12104-017-9730-2
PMID: 28236226
PMCID: PMC5385707
NLM abbreviation: Biomol NMR Assign
ISSN: 1874-2718
eISSN: 1874-270X
Publisher: Netherlands
Grant note: R01 EY010843 / NEI NIH HHS
Language: English
Date published: 04/2017
Academic Unit: Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Biochemistry and Molecular Biology; Medicine Administration; Ophthalmology and Visual Sciences
Record Identifier: 9984025316402771

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