Fig. 3: The interaction specificity between EDA·A1THD and EDARCRDS. | Nature Communications

Fig. 3: The interaction specificity between EDA·A1THD and EDARCRDS.

From: Structural insights into pathogenic mechanism of hypohidrotic ectodermal dysplasia caused by ectodysplasin A variants

Fig. 3

a Residue Glu308 in EDA·A1THD exhibits no direct interaction with EDARCRDS. EDA·A1THD is shown in electrostatic potential surface representation with residue Glu308 denoted by a dashed green circle. The EDARCRDS is shown in cartoon mode. b Structural comparison of EDA·A1THD and EDA·A2THD. The structure of EDA·A2THD (PDB: 1RJ8) is superimposed onto the EDA·A1THD-EDARCRDS structure. A close-up view of the interface centered at helix α1 of EDARCRD2 is shown on the right. EDA·A1THD, EDA·A2THD and EDARCRDS are colored in slate blue, cyan, and yellow, respectively. c Structural comparison showing the positional change of Phe314 and Ile336 in EDA·A2THD. d Superposition of the predicted XEDARCRDS generated by AlphaFold (PDB: AF-Q9HAV5) onto the EDA·A1THD-EDARCRDS complex. A close-up view of the interface centered at helix α1 of XEDARCRD2 is shown on the right. EDA·A1THD, EDARCRDS, and XEDARCRDS are colored slate blue, yellow, and hotpink, respectively.

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