Fig. 3: Structural basis of PELP1-PELP1 dimerization. | Nature Communications

Fig. 3: Structural basis of PELP1-PELP1 dimerization.

From: Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold

Fig. 3

a Schematic representation of PELP1’s Rix1 domain with localization of LxxLL and PxxP motifs. Specific motifs involved in PELP1 dimerization, or residing close to dimer interfaces, are noted below the schematic. b Bottom view of segmented cryo-EM density showing two symmetric PELP1 dimerization interfaces between LM81-LM12-LM22 (superscript denotes specific protomer). c Model zoom of LM81-LM12-LM22 dimer interface exhibiting a hydrophobic environment produced by mainly leucine residues from LxxLL motifs. d Top view of cryo-EM density showing a single symmetric PELP1 dimerization interface between LM11 and α-helix 22 of each PELP1 protomer. e Model zoom of LM111+2 - α221+2 interface showing contributing leucine residues to another hydrophobic interface environment.

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