Figure 1.
FIG. 1. The three-dimensional structure of the AIRE1-PHD1
domain. A, multiple sequence alignment of PHD and RING finger
domains. Zinc-binding residues and the conserved Trp are marked
with asterisks (*). Sites of APECED-causing mutations are marked
with a red plus (+). Secondary structure elements of AIRE1-PHD1
are shown above the alignment. B, stereo-view representation of
the backbone atoms (N, C , C') for residues
295-344 of an NMR ensemble of 20 structures. Secondary structure
elements are in blue, the loops and random coil in gray, the
variable loop L3 in yellow, the zinc ions in pink, and the
commonly conserved Trp residue side chain in cyan. C, ribbon
representation of AIRE1-PHD1 (same orientation as B, showing the
side chains (cyan) and atoms (sulfur in yellow, nitrogen in
green) of the zinc-coordinating residues, plus the conserved
Trp335 (cyan).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
11505-11512)
copyright 2005.
, C') for residues
295-344 of an NMR ensemble of 20 structures. Secondary structure
elements are in blue, the loops and random coil in gray, the
variable loop L3 in yellow, the zinc ions in pink, and the
commonly conserved Trp residue side chain in cyan. C, ribbon
representation of AIRE1-PHD1 (same orientation as B, showing the
side chains (cyan) and atoms (sulfur in yellow, nitrogen in
green) of the zinc-coordinating residues, plus the conserved
Trp335 (cyan).