PMID- 11959990
OWN - NLM
STAT- MEDLINE
DCOM- 20020614
LR  - 20220409
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 99
IP  - 8
DP  - 2002 Apr 16
TI  - Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.
PG  - 5367-72
AB  - 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.
FAU - Freedman, Steven J
AU  - Freedman SJ
AD  - Division of Hematology/Oncology, Beth Israel Deaconess Medical Center, 330 
      Brookline Avenue, Boston, MA 02215, USA.
FAU - Sun, Zhen-Yu J
AU  - Sun ZY
FAU - Poy, Florence
AU  - Poy F
FAU - Kung, Andrew L
AU  - Kung AL
FAU - Livingston, David M
AU  - Livingston DM
FAU - Wagner, Gerhard
AU  - Wagner G
FAU - Eck, Michael J
AU  - Eck MJ
LA  - eng
SI  - PDB/1L3E
GR  - K08 HL/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (HIF1A protein, human)
RN  - 0 (Hypoxia-Inducible Factor 1, alpha Subunit)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
RN  - 7006-34-0 (Asparagine)
RN  - J41CSQ7QDS (Zinc)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Asparagine/chemistry
MH  - Escherichia coli/metabolism
MH  - Humans
MH  - Hypoxia-Inducible Factor 1, alpha Subunit
MH  - Magnetic Resonance Spectroscopy
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/*chemistry
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Folding
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Sequence Homology, Amino Acid
MH  - Trans-Activators/*chemistry
MH  - Transcription Factors/*chemistry/metabolism
MH  - Transcriptional Activation
MH  - Zinc/chemistry
PMC - PMC122775
EDAT- 2002/04/18 10:00
MHDA- 2002/06/18 10:01
PMCR- 2002/10/16
CRDT- 2002/04/18 10:00
PHST- 2002/04/18 10:00 [pubmed]
PHST- 2002/06/18 10:01 [medline]
PHST- 2002/04/18 10:00 [entrez]
PHST- 2002/10/16 00:00 [pmc-release]
AID - 99/8/5367 [pii]
AID - 082117899 [pii]
AID - 1178 [pii]
AID - 10.1073/pnas.082117899 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. doi: 10.1073/pnas.082117899.