Figure 3: The molecular interface of the OPTN(26–103)/TBK1 CTD complex. | Nature Communications

Figure 3: The molecular interface of the OPTN(26–103)/TBK1 CTD complex.

From: Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins

Figure 3

(a) Ribbon-stick diagram showing the detailed interior interactions of the OPTN(26–103)/TBK1 CTD complex formed by 10 layers of interacting amino-acid side chains. (b) GST pull-down assays to verify the specific interaction between OPTN NTD and TBK1 CTD, as well as the key binding interface residues. The left panel showing the GST pull-down assay using purified GST-tagged OPTN(26–119) protein and various TBK1 CTD proteins, confirming the crucial interface residues L693 and V700 of TBK1 in binding to OPTN. The right panel showing the GST pull-down assay using purified TBK1 CTD protein and various GST-tagged OPTN(26–119) proteins, confirming the important interface residues M44, L47 and L54 of OPTN in binding to TBK1 CTD. (c) The measured binding affinities between various forms of OPTN and TBK1 proteins or their mutants by ITC-based binding assays. ‘ND’ stands for that the KD value is not detectable. The KD errors are the fitted errors obtained from the data analysis software, when using the one-site binding model to fit the ITC data. The measured N value is related to the binding stoichiometry.

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