Skip to main content
. Author manuscript; available in PMC: 2017 Dec 4.
Published in final edited form as: J Mol Biol. 2016 Oct 27;428(24 Pt B):4981–4992. doi: 10.1016/j.jmb.2016.10.025

Figure 6. GCNF and LRH-1 comparison.

Figure 6

(a) Overlay of GCNF and LRH-1 structures. Molecule 2 of GCNF (Dark purple) sites directly on top of the LRH-1 (orange) recognition site. (b) Close up view of the base-specific contacts mediated by these two receptors. LRH-1 makes an additional contact with Lys 107 making hydrogen bonds to guanine 114. (c) LRH-1 CTE has good electron density, mesh shows 2Fo-Fc electron density map contoured to 1σ around the residues. Arg162 and 165 make hydrogen bonds (red) to thymine 95 and cytosine 110. (d) GCNF CTE has good electron density, mesh shows 2Fo-Fc electron density map contoured to 2σ around the residues. Arg86 makes hydrogen bonds to thymine 109 and cytosine 110. Arg78 also folds into the CTE to make hydrogen bonds to Gly152. (e) Sequence alignment of GCNF and LRH-1 CTEs show LRH-1 to contain two additional Arg residues that are used for DNA binding. (f) Mutational analysis of CTE residues on Oct4 binding: GCNF DBD Gly149Arg/Pro151Arg (open purple circles) bound to the Oct4 DR0 with an affinity 20 nM, where WT GCNF DBD (faded closed purple circles) binds with an affinity of 170 nM. LRH-1 DBD Arg160Gly/Arg162Pro (open orange circles) bound with an affinity of 750 nM, where WT LRH-1 DBD (faded closed orange circles) bound with an affinity of 60 nM.