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Literature summary for 2.3.1.48 extracted from

  • Banerjee, S.; M, A.; Rakshit, T.; Roy, N.S.; Kundu, T.K.; Roy, S.; Mukhopadhyay, R.
    Structural features of human histone acetyltransferase p300 and its complex with p53 (2012), FEBS Lett., 586, 3793-3798.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
visualization of multifunctional transcription activator p300 by atomic force microscopy. p300 is almost prolate ellipsoidal in shape, having several bulges. The functionally significant N-terminal and C-terminal regions are located near one end and centre of the molecule, respectively. The presence of N- and C-terminal regions near the central portion of the prolate ellipsoid suggests that all four domain could exist spatially close near the central portion of the molecule and hence capable of binding all four domains simultaneously. The complex between p300 and tumor suppressor protein p53 is elongated in shape. p53 binds at the central region of p300 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Synonyms

Synonyms Comment Organism
p300
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Homo sapiens