Figure 4.
FIG. 4. Model of RAG2-PtdInsP interactions. A, structural
overlay of the RAG2 PHD finger (green) on the EEA1 FYVE
finger-IP(1,3)[2] complex (FYVE domain, magenta; inositol
1,3-P[2], yellow). (Protein Data Bank code 1HYI [PDB]
(46).) The conserved -sheet and zinc ions
were used to overlay the two structures. Arginine side chains
important for FYVE-PtdInsP binding are shown in magenta. Basic
residues of RAG2 in the L2 segment (Arg-464 and His-468) are
shown in blue. B, ribbon schematic of the RAG2 PHD finger
structure with the indicated basic residues (blue) and
disease-linked residues (red). C, schematic comparison of RAG2
and ING2 C termini. PHD fingers are shown in green. The blue
boxes denote regions of positively charged residues important
for PtdInsP binding by ING2. The analogous regions of RAG2 (L2
and CT) are also highlighted in blue, with the one inside the
PHD finger (L2) corresponding to the blue -helix region in B.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
28701-28710)
copyright 2005.
-sheet and zinc ions
were used to overlay the two structures. Arginine side chains
important for FYVE-PtdInsP binding are shown in magenta. Basic
residues of RAG2 in the L2 segment (Arg-464 and His-468) are
shown in blue. B, ribbon schematic of the RAG2 PHD finger
structure with the indicated basic residues (blue) and
disease-linked residues (red). C, schematic comparison of RAG2
and ING2 C termini. PHD fingers are shown in green. The blue
boxes denote regions of positively charged residues important
for PtdInsP binding by ING2. The analogous regions of RAG2 (L2
and CT) are also highlighted in blue, with the one inside the
PHD finger (L2) corresponding to the blue 
-helix region in B.