1H, 13C and 15N backbone resonance assignments and dynamic properties of the PDZ tandem of Whirlin

Autor: Florence Cordier, Nicolas Wolff, Florent Delhommel
Přispěvatelé: Résonance Magnétique Nucléaire des Biomolécules, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Cellule Pasteur UPMC, Institut Pasteur [Paris]-Sorbonne Université (SU), This work was supported by the Programme Transversal de Recherche from the Institut Pasteur (PTR Grant No. 483) and the Ministère de l’Enseignement Supérieur et de la Recherche (Grant No. 883/2013 to F.D.). Financial support from the TGIR-RMN-THC Fr3050 CNRS for conducting the research is gratefully acknowledged., We thank F.X. Cantrelle (UCCS-UGSF, Lille) and C. Simenel (NMR unit, Institut Pasteur) for their NMR technical expertise and helpful discussions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Sorbonne Université (SU)
Jazyk: angličtina
Rok vydání: 2016
Předmět:
0301 basic medicine
Scaffold protein
PDZ tandem
MESH: PDZ Domains
[SDV]Life Sciences [q-bio]
PDZ domain
PDZ Domains
MESH: Protein Structure
Secondary
Mechano-electrical transduction
Whirlin
Biochemistry
Protein Structure
Secondary
MESH: Membrane Proteins / chemistry
Backbone resonance assignments
03 medical and health sciences
Mice
Structural Biology
MESH: Membrane Proteins / metabolism
medicine
otorhinolaryngologic diseases
Animals
PDZ
MESH: Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Protein secondary structure
Nuclear Magnetic Resonance
Biomolecular
MESH: Mice
030102 biochemistry & molecular biology
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Cadherin
Chemistry
MESH: Nuclear Magnetic Resonance
Biomolecular
Membrane Proteins
Depolarization
biology.organism_classification
Crystallography
030104 developmental biology
medicine.anatomical_structure
Membrane protein
Talos
Biophysics
Hair cell
sense organs
Zdroj: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
Biomolecular NMR Assignments, 2016, 10 (2), pp.361-365. ⟨10.1007/s12104-016-9701-z⟩
ISSN: 1874-270X
DOI: 10.1007/s12104-016-9701-z⟩
Popis: International audience; Mammals perceive sounds thanks to mechanosensory hair cells located in the inner ear. The stereocilia of these cells are tightly bound together in bundles by a network of cadherins and scaffolding proteins. Stereocilia deflection induces stretching of this network and is responsible for hair cell depolarization that triggers the neuronal message, transducing the mechanical signal into an electric signal transmissible to the brain. Nearly all proteins involved in this mechano-electrical transduction network contain short C-terminal motifs of interaction with PDZ domains (PSD-95, Discs Large, ZO-1). Interestingly only two of these proteins encompass PDZ domains: Harmonin and Whirlin. As our first step towards a comprehensive structural study of Whirlin, we have assigned the (1)H, (13)C and (15)N backbone resonances of a tandem formed by the first two PDZ domains of Whirlin, reported the secondary structure elements of this tandem as predicted by the TALOS+ server and evaluated its dynamics from (15)N relaxation measurements.
Databáze: OpenAIRE
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