Hypoxia-Inducible factor 1 alpha inhibitor

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**[[2wa3]], [[2wa4]], [[3od4]], [[4ai8]], [[5op6]], [[5op8]], [[5opc]] – hFIH-1 + inhibitor <br />
**[[2wa3]], [[2wa4]], [[3od4]], [[4ai8]], [[5op6]], [[5op8]], [[5opc]] – hFIH-1 + inhibitor <br />
**[[1yci]] – hFIH-1 + Phe derivative<br />
**[[1yci]] – hFIH-1 + Phe derivative<br />
-
**[[2xum]] – hFIH-1 (mutant) + peptide<br />
+
**[[1h2n]], [[1mzf]], [[2w0x]], [[2yc0]], [[2yde]], [[4z2w]], [[7a1j]], [[7a1k]], [[7a1l]], [[7a1m]] – hFIH-1 + glutarate derivative<br />
-
**[[1h2n]], [[1mzf]], [[2w0x]], [[2yc0]], [[2yde]], [[4z2w]] – hFIH-1 + glutarate derivative<br />
+
**[[5jwk]], [[5jwl]] – hFIH-1 (mutant) + glutarate derivative<br />
**[[5jwk]], [[5jwl]] – hFIH-1 (mutant) + glutarate derivative<br />
**[[4z1v]] – hFIH-1 + oxalylglycine<br />
**[[4z1v]] – hFIH-1 + oxalylglycine<br />
Line 35: Line 34:
*Hypoxia-inducible factor 1 alpha inhibitor complex with peptide
*Hypoxia-inducible factor 1 alpha inhibitor complex with peptide
 +
**[[2xum]] – hFIH-1 (mutant) + peptide<br />
**[[1h2l]] – hFIH-1 + HIF-1 peptide + glutarate derivative<br />
**[[1h2l]] – hFIH-1 + HIF-1 peptide + glutarate derivative<br />
**[[2ilm]], [[3d8c]], [[5jwp]] – hFIH-1 (mutant) + HIF-1 peptide + glutarate derivative<br />
**[[2ilm]], [[3d8c]], [[5jwp]] – hFIH-1 (mutant) + HIF-1 peptide + glutarate derivative<br />
-
**[[2y0i]] – hFIH-13 + tankyrase-2 peptide + glutarate derivative<br />
+
**[[2y0i]], [[7a1s]] – hFIH-13 + tankyrase-2 peptide + glutarate derivative<br />
**[[3p3n]], [[3p3p]] – hFIH-1 + notch 1 peptide + glutarate derivative<br />
**[[3p3n]], [[3p3p]] – hFIH-1 + notch 1 peptide + glutarate derivative<br />
**[[4z1v]] – hFIH-1 + oxalylglycine<br />
**[[4z1v]] – hFIH-1 + oxalylglycine<br />
Line 46: Line 46:
**[[6hkp]] – hFIH-1 + ASPP2 peptide + oxalylglycine<br />
**[[6hkp]] – hFIH-1 + ASPP2 peptide + oxalylglycine<br />
**[[4b7e]], [[4b7k]], [[4jaa]], [[4rn1]], [[6ruj]] – hFIH-1 + concensus Ankyrin-repeat domain peptide + oxalylglycine<br />
**[[4b7e]], [[4b7k]], [[4jaa]], [[4rn1]], [[6ruj]] – hFIH-1 + concensus Ankyrin-repeat domain peptide + oxalylglycine<br />
 +
**[[7a1n]], [[7a1o]], [[7a1p]], [[7a1q]] – hFIH-1 + concensus Ankyrin-repeat domain peptide + oxoglutaraste derivative<br />
}}
}}
== References ==
== References ==

Revision as of 10:07, 30 September 2021

Structure of FIH-1 dimer (cyan, green) complex with HIF-1 C-terminal transactivation domain (pink, magenta), oxalylglycine, sulphate and Zn+2 ion (grey) (PDB code 1h2m)

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3D Structures of Hypoxia-Inducible factor 1 alpha inhibitor

Updated on 30-September-2021

References

  1. Mahon PC, Hirota K, Semenza GL. FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 2001 Oct 15;15(20):2675-86. PMID:11641274 doi:http://dx.doi.org/10.1101/gad.924501
  2. Kiriakidis S, Henze AT, Kruszynska-Ziaja I, Skobridis K, Theodorou V, Paleolog EM, Mazzone M. Factor-inhibiting HIF-1 (FIH-1) is required for human vascular endothelial cell survival. FASEB J. 2015 Jul;29(7):2814-27. doi: 10.1096/fj.14-252379. Epub 2015 Apr 2. PMID:25837583 doi:http://dx.doi.org/10.1096/fj.14-252379
  3. Chen T, Ren Z, Ye LC, Zhou PH, Xu JM, Shi Q, Yao LQ, Zhong YS. Factor inhibiting HIF1alpha (FIH-1) functions as a tumor suppressor in human colorectal cancer by repressing HIF1alpha pathway. Cancer Biol Ther. 2015;16(2):244-52. doi: 10.1080/15384047.2014.1002346. PMID:25602156 doi:http://dx.doi.org/10.1080/15384047.2014.1002346
  4. Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. J Biol Chem. 2003 Jan 17;278(3):1802-6. Epub 2002 Nov 21. PMID:12446723 doi:http://dx.doi.org/10.1074/jbc.C200644200

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