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Figure 6
Lysine cross-linking indicates that the C-terminal and N-terminal IDRs make contact with the DBHS domain. (a) Lysine cross-links detected via mass spectrometry in full-length SFPQ at 0.7 mg ml−1 (10 µM). Cross-links are connected via a line across the amino-acid sequence. Black indicates links involving the C-terminal IDR, purple indicates cross-links within the DBHS domain, red indicates cross-links involving the N-terminal IDR and gold indicates cross-links between the same peptide. (b) Cross-links detected for SFPQ1–598 (20 µM). (c) The DBHS domain is coloured marine and the C-terminal IDR is coloured grey; points of contact are indicated by a yellow line between the DBHS domain, the coiled-coil domain and the C-terminal IDR. The enlarged DBHS dimer indicates lysines involved in cross-linking (purple). The equivalent position of NONO C145 (Thr368 in SFPQ) has been highlighted in yellow. This may form disulfides with disease-associated cysteine mutants in the C-terminal IDRs of DBHS proteins (see Section 4.4[link]).

Journal logo STRUCTURAL
BIOLOGY
ISSN: 2059-7983
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