1L3E

NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex

Summary for 1L3E

• Entry DOI: 10.2210/pdb1l3e/pdb
• NMR Information: BMRB: 5306
• Descriptor: hypoxia inducible factor-1 alpha subunit, p300 protein, ZINC ION (3 entities in total)
• Functional Keywords: protein-protein complex, transcription
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q16665 Q09472
• Total number of polymer chains: 2
• Total formula weight: 16185.50

Authors

Freedman, S.J.,Sun, Z.J.,Poy, F.,Kung, A.L.,Livingston, D.M.,Wagner, G.,Eck, M.J. (deposition date: 2002-02-26, release date: 2002-04-24, Last modification date: 2024-11-13)

Primary citation

Freedman, S.J.,Sun, Z.Y.,Poy, F.,Kung, A.L.,Livingston, D.M.,Wagner, G.,Eck, M.J.
Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.
Proc.Natl.Acad.Sci.USA, 99:5367-5372, 2002

PubMed Abstract: Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators. We report the solution structure of the cysteine/histidine-rich 1 (CH1) domain of p300 bound to the C-terminal transactivation domain of HIF-1 alpha. CH1 has a triangular geometry composed of four alpha-helices with three intervening Zn(2+)-coordinating centers. CH1 serves as a scaffold for folding of the HIF-1 alpha C-terminal transactivation domain, which forms a vise-like clamp on the CH1 domain that is stabilized by extensive hydrophobic and polar interactions. The structure reveals the mechanism of specific recognition of p300 by HIF-1 alpha, and shows how HIF-1 alpha transactivation is regulated by asparagine hydroxylation.

PubMed: 11959990
DOI: 10.1073/pnas.082117899

Experimental method

SOLUTION NMR