Double-hydroxylated HIF-1alpha oxygen-dependent degradation domain

(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid

Proceedings of the National Academy of Sciences of the United States of America
Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1α.

The two "X" in the sequence denote 4-hydroxyproline.
It starts from 394 (P394) and ends at 574 (L574)

A master transcriptional regulator of the adaptive response to hypoxia with protein stability mediated by prolyl hydroxylation in the oxygen-dependent manner.

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Chemical shift backbone assignment of the oxygen-dependent degradation domain of
human HIF-1alpha (residues 394-574), with two hydroxyprolines on at positions of
402 and 564.

We also conducted 13C-detected 2D CON experiments for the assignment of 15N values of proline residues.

HIF-1alpha oxygen-dependent degradation domain