Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1

Berger et al. 10.1073/pnas.0609211104.

Supporting Information

Files in this Data Supplement:

SI Figure 6




Fig. 6. The 3D structure of the NMN adenylyl transferase 1 (NMNAT-1) monomer (Protein Data Bank ID no.: 1KQN:A). The exit and entry points of the S136-containing loop are represented by the C-a atoms of A108 (lower left) and A147 (shown in space fill). The residues of the potential poly(ADP-ribose) (PAR) binding site motif are shown as sticks (amino acids 56-75). The N terminus of the motif is at lower left. The distance between the loop exit/entry points and the motif (C-terminus) is 26-27 Å. There are 10 amino acid residues between A147 and S136. If the structure of this region were fully extended, it would cover a distance of 76 Å. Consequently, the potential PAR binding motif could interact with both polymers and the loop containing S136. Therefore, phosphorylation of S136 could interfere with PAR binding.

This Article

  1. Published online before print February 22, 2007, doi: 10.1073/pnas.0609211104 PNAS March 6, 2007 vol. 104 no. 10 3765-3770
  1. AbstractFree
  2. Figures Only
  3. Full Text
  4. Full Text (PDF)
  5. » Supporting Figure
About Our New Site Design >>
Link: Advanced Search

This Week's Issue

  1. November 11, 2008, 105 (45)
  1. Current Issue
  1. Alert me to new issues of PNAS

Most