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![[Figure 1]](ag5054fig1mag.jpg)
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Figure 1
The DBHS family, dimerization and disorder. (a) The domain map of the DBHS family indicates the conserved central DBHS region coloured by domain (gold for RRM1, blue for RRM2, orange for NOPS and red for the coiled-coil domain). The different IDRs and the DBD are coloured grey. (b) Side view and top view of the structure of an SFPQ homodimer (PDB entry 4wii; Lee et al., 2015  ). The protein variant was truncated to remove the extended coiled-coil domain and disordered regions. This structure has been coloured according to the domain map in (a). (c) Predicted AlphaFold2 (Mirdita et al., 2022) structure of human full-length SFPQ coloured according to the domain map in (a). One monomer in the dimer is shown as a cartoon representation and the other as a surface representation without IDRs for simplicity. Light grey regions are the N- and C-terminal IDRs represented as `barbed wire' by AlphaFold. Below the predicted structure AlphaFold pLDDT and PLAAC prion-like probability (Lancaster et al., 2014) scores for human SFPQ as a function of amino-acid number are shown. A pLDDT score above ∼50 is a good indicator of structure and a score below ∼50 is indicative of disorder. A PLAAC score approaching 1 (100) is indicative of prion-like characteristics/sequence. |
![[Figure 1]](ag5054fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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