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Figure 6 | BMC Genomics

Figure 6

From: Conserved and variable correlated mutations in the plant MADS protein network

Figure 6

Structural implications of intermolecular correlated mutations for MADS proteins. (A) Intermolecular correlated mutations between K-domain helices do not support an "extended helix organization" (left panel), but suggest a more compact configuration (right panel). (B) Correlated mutation results support motif-based predicted interaction site. Predicted K-domain coiled coil regions (black lines), overlaid with predicted correlated mutation positions complementary to the 'hotspot region' in SOC1, for SEP1 and SHP1 (red circles). Most of the correlated mutation positions fall inside the first K-domain helix (green shade); based on motif predictions in combination with structural information, an interaction between the 'hotspot' region and the K-domain was hypothesized, for which the correlated mutation results provide additional support.

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