| Primary Identifier | IPR056167 | Type | Domain |
| Short Name | A-sol_ELP1 |
| description | This entry represents the ��-solenoid domain found within the C-terminal dimerisation domain of Elongator complex protein 1 (ELP1) from eukaryotes. Residues within the ��-14-helix are highly conserved from yeast to human and act as a kink to maintain the TPR-like domain and ��-solenoid domain at nearly a 90-degree angle.Elongator is a conserved protein complex implicated in multiple processes including regulation of transcription, alpha-tubulin acetylation and tRNA modification. Mutations in the ELP1 gene have been shown to cause the neurodegenerative disease familial dysautonomia []. The C-terminal dimerisation domain consists of 28 ��-helices organised in three domains: an elongated ��-solenoid domain (helices 1 to 14); a TPR domain, formed by six double-helix repeats (helices 15 to 26); and a three-helix bundle, C-terminal cap (helices 26 to 28) []. ELP1 self-association contributes to its stability and is important for Elongator assembly []. ELP1 is considered to function both as a scaffold, for Elongator complex ELP2 and ELP3 binding, and as a docking site for various factors that regulate Elongator activity [, , ]. Also known as IKAP, ELP1 acts as a regulator of IkB kinase complex involved in proinflammatory cytokine signalling []. |
