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Pisces3rule

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E cullin protein. (E) The APC/C complex shows a greater diversity compare to the other classes of cullin-based E3 ligases due to the nature of this complex to utilize at least 11 subunits in addition to using a cullin- and an RBX1-like protein (APC2 and APC11 respectively) as the core scaffolding unit.CUL1-BASED E3 LIGASES Complex composition and structural organization of the different subunits P
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E cullin protein. (E) The APC/C complex shows a greater diversity compare to the other classes of cullin-based E3 ligases due to the nature of this complex to utilize at least 11 subunits in addition to using a cullin- and an RBX1-like protein (APC2 and APC11 respectively) as the core scaffolding unit.CUL1-BASED E3 LIGASES Complex composition and structural organization of the different subunits P
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E cullin protein. (E) The APC/C complex shows a greater diversity compare to the other classes of cullin-based E3 ligases due to the nature of this complex to utilize at least 11 subunits in addition to using a cullin- and an RBX1-like protein (APC2 and APC11 respectively) as the core scaffolding unit.CUL1-BASED E3 LIGASES Complex composition and structural organization of the different subunits P
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Ullin-repeats. Each of these repeats are composed of a five-helix structural motif in which the helices C to E are organized as a three-helix bundle that interacts with helices A and B to form the cullin repeat (Zheng et al., 2002b). Specifically the first repeat is responsible for binding the substrate adaptor complex of SkpCullin-based Ubiquitin E3 Ligases3 ofand the F-box protein, while the oth
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Ullin-repeats. Each of these repeats are composed of a five-helix structural motif in which the helices C to E are organized as a three-helix bundle that interacts with helices A and B to form the cullin repeat (Zheng et al., 2002b). Specifically the first repeat is responsible for binding the substrate adaptor complex of SkpCullin-based Ubiquitin E3 Ligases3 ofand the F-box protein, while the oth
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Six cullin-like proteins, CULLIN1 (CUL1: At4g02570), CULLIN2 (further referred to here as CUL1b: At1g02980 to avoid confusion with human Cul2), CULLIN3a (CUL3a: At1g25830), CULLIN3b (CUL3b: At1g69670), CULLIN4 (CUL4: At5g46210), and ANAPHASE PROMOTING COMPLEX2 (APC2: At2g04660). They range in size from 85 to 98 kDa, and are all characterized by a conserved cullin-region ofaround 200 amino acids in
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Six cullin-like proteins, CULLIN1 (CUL1: At4g02570), CULLIN2 (further referred to here as CUL1b: At1g02980 to avoid confusion with human Cul2), CULLIN3a (CUL3a: At1g25830), CULLIN3b (CUL3b: At1g69670), CULLIN4 (CUL4: At5g46210), and ANAPHASE PROMOTING COMPLEX2 (APC2: At2g04660). They range in size from 85 to 98 kDa, and are all characterized by a conserved cullin-region ofaround 200 amino acids in
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Six cullin-like proteins, CULLIN1 (CUL1: At4g02570), CULLIN2 (further referred to here as CUL1b: At1g02980 to avoid confusion with human Cul2), CULLIN3a (CUL3a: At1g25830), CULLIN3b (CUL3b: At1g69670), CULLIN4 (CUL4: At5g46210), and ANAPHASE PROMOTING COMPLEX2 (APC2: At2g04660). They range in size from 85 to 98 kDa, and are all characterized by a conserved cullin-region ofaround 200 amino acids in