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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.

Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA - Biomol NMR Assign (2011)

Bottom Line: Neuroligins act as heterophilic adhesion molecules at neuronal synapses.Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered.Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

View Article: PubMed Central - PubMed

Affiliation: Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.

ABSTRACT
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

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Related in: MedlinePlus

Predicted intrinsic exchange rates of amide protons with solvent for hNL3-cyt at pH 6.0, 25°C. pKa values of 4.0 for Asp, 4.4 for Glu, and 6.75 for His side chains were used. Residues H20, H64, S133, H134, and S135 have predicted exchange rates faster than 15 s−1; Except for S133, which is broadened, their amide resonances are not visible in the spectra
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Fig2: Predicted intrinsic exchange rates of amide protons with solvent for hNL3-cyt at pH 6.0, 25°C. pKa values of 4.0 for Asp, 4.4 for Glu, and 6.75 for His side chains were used. Residues H20, H64, S133, H134, and S135 have predicted exchange rates faster than 15 s−1; Except for S133, which is broadened, their amide resonances are not visible in the spectra

Mentions: To understand whether the absence of some backbone amide proton resonances in our experiments was due to fast exchange with the solvent, intrinsic exchange rates were calculated (Bai et al. 1993) using the program Sphere (http://www.fccc.edu/research/labs/roder/sphere/sphere.html) and these values are plotted in Fig. 2. The data show that in all cases where the amide proton resonance was not assigned (for residues H20, H64, H134, and S135), intrinsic exchange rates faster than 15 s−1 are predicted.Fig. 2


Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.

Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA - Biomol NMR Assign (2011)

Predicted intrinsic exchange rates of amide protons with solvent for hNL3-cyt at pH 6.0, 25°C. pKa values of 4.0 for Asp, 4.4 for Glu, and 6.75 for His side chains were used. Residues H20, H64, S133, H134, and S135 have predicted exchange rates faster than 15 s−1; Except for S133, which is broadened, their amide resonances are not visible in the spectra
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3298649&req=5

Fig2: Predicted intrinsic exchange rates of amide protons with solvent for hNL3-cyt at pH 6.0, 25°C. pKa values of 4.0 for Asp, 4.4 for Glu, and 6.75 for His side chains were used. Residues H20, H64, S133, H134, and S135 have predicted exchange rates faster than 15 s−1; Except for S133, which is broadened, their amide resonances are not visible in the spectra
Mentions: To understand whether the absence of some backbone amide proton resonances in our experiments was due to fast exchange with the solvent, intrinsic exchange rates were calculated (Bai et al. 1993) using the program Sphere (http://www.fccc.edu/research/labs/roder/sphere/sphere.html) and these values are plotted in Fig. 2. The data show that in all cases where the amide proton resonance was not assigned (for residues H20, H64, H134, and S135), intrinsic exchange rates faster than 15 s−1 are predicted.Fig. 2

Bottom Line: Neuroligins act as heterophilic adhesion molecules at neuronal synapses.Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered.Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

View Article: PubMed Central - PubMed

Affiliation: Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.

ABSTRACT
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

Show MeSH
Related in: MedlinePlus