![]() Two additional α-helix-loop-α-helix regions were detected in 680 the N-terminal SRD. The six ankyrin repeat units of the ARD are recovered, correctly 679 annotated and positioned. Truncated, as crystallized IκBα from 1IKN (residues 73-293) is shown 678 in bold letters. 675 676 Figure 3: Consensus secondary structure annotation of full length IκBα 677 (residues 1-317). The diversity of binding sites, 672 the great variability of κB-sites in the DNA motif and the existence of suppressive and 673 inductive NF-κB dimers lead to a complexity and versatility of the downstream 674 signaling network. Indicated for the C-terminal 671 PEST-like region are the CKII sites of phosphorylation. The 669 ankyrin repeat units in the protein crystal structure of IκBα in complex with NF-κB 670 (pdb entry 1IKN) are shown as a cartoon representation. The N-terminal 667 SRD is the site of phosphorylation by IKK and subsequent ubiquitination by the SCF 668 (β-TrCP) E3 ligase, six ankyrin repeat units make up the central ARD domain. 665 666 Figure 2: Schematic representation of protein domains in IκBα. This activates NF-κB whereas 664 IκBα is degraded in the 26S proteasome. Phosphorylation by IKK leads to a degron, recognized by 663 SCF(β-TrCP) and subsequent IκBα ubiquitination by E3. Stabilization of IκBα upon protein-protein complex formation with the 662 transcription factor NF-κB. ![]()
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