Synthesis and biochemical evaluation of O-acetyl-ADP-ribose and N-acetyl analogs

Organic and Biomolecular Chemistry

Volumn 5, Issue 19, 2007, Pages 3087-3091

  Comstock, Lindsay R ^a   Denu, John M ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; SUGAR (SUCROSE); SYNTHESIS (CHEMICAL);

HISTONE; N-ACETYL ANALOGS; O-ACETYL-ADP-RIBOSE;

PHOSPHATES;

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSE ACETATE; SIRTUIN;

ACETYLATION; ARTICLE; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM;

ACETYLATION; ADENOSINE DIPHOSPHATE RIBOSE; MODELS, MOLECULAR; O-ACETYL-ADP-RIBOSE; SIRTUINS;

EID: 34548732389     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/b710231c     Document Type: Article

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45. The structure of macroH2A1.1 was not co-crystallized with OAADPr. Thus, the crystal structure of ADPr bound to the Af1521 macro domain (PDB accession code 2BFQ) was overlayed with macroH2A1.1 (carbon backbone was matched based upon homology) and the resulting structure of ADPr was utilized as a starting point for modeling the N-acetyl analogs into macroH2A1.1. The structure of ADPr was modified in SYBYL, torsionally constrained about the new bonds, and energies minimized across the new structure. PyMol was utilized to produce the images in Fig. 4.
46. Previous studies of the Af1521 macro domain bound to ADPr indicated that mutation of Asn 34 to Ala reduced binding affinity three-fold. See ref. 32.