| Type: | Domain | Name: | Hypoxia-inducible factor 1-alpha inhibitor, domain II |
| Description: | This entry represents the domain II of the hypoxia-inducible factor 1-alpha inhibitor, which is composed of a central beta-barrel surrounded by eight alpha-helices. It consists of two domains. Domain I runs from N terminus to residue 300 and is mainly composed of the central beta-barrel and six alpha-helices surrounding them. Domain II (residues 301-349) comprising two consecutive alpha-helices stretches away from domain I. Domain II, which is completely missing in all known structures of the dioxygenase family, forms strong interactions with the same region of the 2-fold symmetry related molecule [, , ]. Hypoxia-inducible factor 1-alpha inhibitor hydroxylates a specific Asn residue in the C-terminal transactivation domain (CAD) of HIF-1 alpha. The hydroxylation prevents interaction of HIF-1 with transcriptional coactivators. It also hydroxylates specific Asn, Asp and His residues within ankyrin repeat domain-containing proteins [, , ]. | Short Name: | FIH-1_domII |
