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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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Structure prediction for hNL3-cyt based on sequence similarity using Jpred 3. Most residues are predicted to be disordered (indicated by dashed line), but three short helical segments are predicted
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Fig4: Structure prediction for hNL3-cyt based on sequence similarity using Jpred 3. Most residues are predicted to be disordered (indicated by dashed line), but three short helical segments are predicted

Mentions: Figure 1 illustrates the 2D [1H–15N]-HSQC spectrum and assignments of the amide resonances of hNL3-cyt; its unfolded nature is evident from the small dispersion in the amide proton resonances. The construct contains 139 residues, the first 10 of which are a 6xHis-tag, followed by a short linker sequence (see also Fig. 4). Following a standard sequential assignment procedure, 98% of the observable backbone 1H, 15N and 13C resonances were assigned (excluding the tag). The observable 1H/15N pairs are displayed in Fig. 1, labeled by their one-letter amino acid code and residue number. Considering only aliphatic 1H and 13C atoms, side chain assignments are complete to 92%.Fig. 1


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)

Structure prediction for hNL3-cyt based on sequence similarity using Jpred 3. Most residues are predicted to be disordered (indicated by dashed line), but three short helical segments are predicted
© Copyright Policy
Related In: Results  -  Collection

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

Fig4: Structure prediction for hNL3-cyt based on sequence similarity using Jpred 3. Most residues are predicted to be disordered (indicated by dashed line), but three short helical segments are predicted
Mentions: Figure 1 illustrates the 2D [1H–15N]-HSQC spectrum and assignments of the amide resonances of hNL3-cyt; its unfolded nature is evident from the small dispersion in the amide proton resonances. The construct contains 139 residues, the first 10 of which are a 6xHis-tag, followed by a short linker sequence (see also Fig. 4). Following a standard sequential assignment procedure, 98% of the observable backbone 1H, 15N and 13C resonances were assigned (excluding the tag). The observable 1H/15N pairs are displayed in Fig. 1, labeled by their one-letter amino acid code and residue number. Considering only aliphatic 1H and 13C atoms, side chain assignments are complete to 92%.Fig. 1

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