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. 2018 Nov 21;115(50):12781–12786. doi: 10.1073/pnas.1803826115

Fig. 1.

Fig. 1.

SdY conserves the structure of the IRF protein–protein interaction domain and interacts with the Forkhead box domain of Fox proteins. (A) SdY shares structural homologies with IAD, a protein–protein interaction domain. The structure of SdY (in gray) was modeled using the crystal structure of IRF5 as a template (in green). This SdY structure reveals eight β-sheets forming a β-sandwich and three α-helices that are highly conserved with IRF5. (B) SdY interacts in yeast with Fox proteins through their highly conserved DNA-binding domain. The alignments of the SdY-Fox interacting clone sequences (gray lines) delineate the minimum domain or selected interacting domain needed for an effective interaction with SdY in yeast, which is the Forkhead box domain (110 aa, black lines). The 11 Fox proteins characterized in the Y2H screen are represented by open cylinders with numbers of interacting clones indicated on the right side.