Histone acetyltransferase

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Line 49: Line 49:
**[[2ln0]] - hHAT KAT6A<br />
**[[2ln0]] - hHAT KAT6A<br />
**[[4ljn]] - hHAT KAT6A double PHD finger<br />
**[[4ljn]] - hHAT KAT6A double PHD finger<br />
 +
**[[5j8c]], [[5j8f]] - hHAT KAT8 residues 177-447 (mutant)<br />
**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''
**[[2qec]] – HAT HPA2 (mutant) – ''Corynebacterium glutamicum''
Line 74: Line 75:
**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
**[[4pzr]], [[4pzs]] - hHAT P300 acetyltransferase domain (mutant) + acetyl CoA<br />
**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
**[[4pzt]] - hHAT P300 acetyltransferase domain (mutant) + acetonyl CoA<br />
-
 
+
**[[5lkt]] - hHAT P300 residues 1581-1666 + butyryl CoA<br />
 +
**[[5lku]] - hHAT P300 catalytic core + CoA<br />
 +
**[[5lkx]] - hHAT P300 catalytic core (mutant) + propionyl CoA<br />
 +
**[[5lkz]] - hHAT P300 catalytic core (mutant) + crotonyl CoA<br />
 +
**[[5bt3]] - hHAT P300 bromodomain + inhibitor<br />
**[[1wug]], [[1wum]] – hHAT PCAF + small ligand
**[[1wug]], [[1wum]] – hHAT PCAF + small ligand
Line 84: Line 89:
**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
**[[2rnw]], [[2rnx]] - hHAT PCAF bromodomain + histone H3 peptide - NMR<br />
 +
**[[5h84]] - hHAT KAT2A + propionyl CoA<br />
 +
**[[5h86]] - hHAT KAT2A + butyryl CoA<br />
 +
**[[5lvq]], [[5lvr]], [[5fdz]], [[5fe0]], [[5fe1]], [[5fe2]], [[5fe3]], [[5fe4]], [[5fe5]], [[5fe6]], [[5fe7]], [[5fe8]], [[5fe9]] - hHAT KAT2B bromodomain + inhibitor<br />
**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
**[[4dnc]] – hHAT KAT8 HAT domain + male-specific lethal 1 homolog<br />
-
**[[3v43]], [[4lk9]], [[4lka]]. [[4llb]] - hHAT KAT6A + H3.1 peptide<br />
+
**[[3v43]], [[4lk9]], [[4lka]]. [[4llb]], [[5b75]], [[5b76]], [[5b77]], [[5b78]] - hHAT KAT6A + H3.1 peptide<br />
 +
**[[5u2j]] - hHAT KAT6B + H3K14BU peptide<br />
 +
**[[5gk9]] - hHAT KAT7 + BRD1<br />
 +
**[[5tpx]] - HAT GCN5 + probe – ''Plasmodium falciparum''<br />
*Histone acetyltransferase ternary complexes
*Histone acetyltransferase ternary complexes
-
**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide
+
**[[3q33]] – yHAT RTT109 + vacuolar protein sorting-associated protein 75 + histone H3 peptide<br />
 +
**[[4psx]] - yHAT B + H3 peptide + H4 peptide<br />
 +
**[[5j9q]], [[5j9t]], [[5j9u]], [[5j9w]] - yHAT Esa1 (mutant) + chromatin modification-related protein + enhancer of polycomb-like protein<br />
**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide
**[[1q2c]] - TtHAT Gcn5 + CoA + histone H4 peptide

Revision as of 10:35, 12 June 2017

Yeast histone acetyltransferase complex with acetyl CoA and Ca+2 ion (green) (PDB entry 1bob)

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3D Structures of histone acetyltransferase

Updated on 12-June-2017

References

  1. Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81-120. PMID:11395403 doi:10.1146/annurev.biochem.70.1.81
  2. Dekker FJ, van den Bosch T, Martin NI. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov Today. 2014 May;19(5):654-60. doi: 10.1016/j.drudis.2013.11.012. Epub, 2013 Nov 21. PMID:24269836 doi:http://dx.doi.org/10.1016/j.drudis.2013.11.012
  3. Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
  4. Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 1998 Aug 21;94(4):427-38. PMID:9727486

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Michal Harel, Alexander Berchansky

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