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. 2007 Feb 27;104(9):3095–3100. doi: 10.1073/pnas.0610548104

Fig. 3.

Fig. 3.

Conserved zinc coordination and core regions of IBR domains. (a) A ribbon structure showing the packing of conserved core hydrophobic residues in Parkin. The structure shows residues V330, A339, and L341 (L1) pack with residues V350 and F364 (L2) allowing formation of a scissor-like arrangement. Two peripheral residues, P343 and R366 provide auxiliary interactions whereas Y372 helps stabilize site II to site I. (b) Multiple sequence alignment of IBR domains from several human paralogs constructed from ClustalW (43) and Jalview (44). Underlined proteins interact with human UbcH7 and UbcH8, whereas RNF14 interacts with UbcH7 alone. Conserved metal binding ligands (yellow) and hydrophobic core residues (green) are highlighted. Residues where mutations have been found in ARJP (open stars) and mutated in this study (filled stars) are indicated.