Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 99, Issue 8, Pages 5367-5372Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.082117899
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- NHLBI NIH HHS [K08 HL] Funding Source: Medline
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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-1alpha. CH1 has a triangular geometry composed of four a-helices with three intervening Zn2+-coordinating centers. CH1 serves as a scaffold for folding of the HIF-1alpha 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-1alpha, and shows how HIF-1alpha transactivation is regulated by asparagine hydroxylation.
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