Parkin: Difference between revisions

Parkin's <scene name='81/817545/Secondary_structure/1'>secondary structure</scene> reveals a compact, autoinhibited conformation. <scene name='81/817545/Ubl_secondary/1'>Ubl domain</scene> is made of 5 strands and 2 helices; <scene name='81/817545/Ring0_secondary_structure/1'>RING0 domain</scene> contains 1 helix and 5 strands; <scene name='81/817545/Ring1_secondary_structure/1'>RING1 domain</scene> is made of 5 strands and 2 helices; The <scene name='81/817545/Ibr_secondary_structure/1'>IBR domain</scene> is composed solely of 3 beta strands; the <scene name='81/817545/Rep_secondary_structure/1'>REP element</scene> consists of an alpha-helix; and the <scene name='81/817545/Ring2_secondary_structure/1'>RING2 domain</scene> is made of 1 alpha-helix and 4 beta-strands. The whole protein is made of 22 beta-strands and 7 alpha-helices. The largest interface in the protein is that between Ubl and the rest of parkin. The <scene name='81/817545/Ubl-ring1_interface/1'>primary contact</scene> is between the Ubl (β3, β5) and RING1 (helix H1) domains, sustained mainly by hydrophobic interactions mediated by I44 and V70 of the Ubl domain and L266, V269 and T270 of the RING1 domain.