Figure 4.
Figure 4 DNA recognition in the NFAT-AP-1-ARRE2 complex. a,
View of the composite binding groove generated by the DNA-facing
surfaces of NFAT, Fos and Jun. The colour scheme indicates
electrostatic potential (blue, positive; red, negative) as
calculated by the program GRASP49. b, Schematic diagram of
detailed protein-DNA contacts, compared with similar contacts in
the NF- B
p50-DNA complex (upper left)24 and in the ternary Fos-Jun-AP-1
site complex (lower right)31. Lines with arrowheads, hydrogen
bonds; lines with filled circles at either end, van der Waals
contacts; solid lines, major-groove and sugar-phosphate
interactions; dashed lines, minor-groove interactions. The
coloured blocks indicate which protein is involved. c, Detailed
view (using Ribbons50) of NFAT interactions in the major groove,
showing the roles of Arg 421, Glu 427, Arg 430, Gln 571 and Arg
572 in specifying base pairs. Arg 430 is supported by salt links
to Glu 427, which also accepts hydrogen bonds from the
main-chain NH of Tyr 424 and from N4 of Cyt 2'. The view is
essentially the same as that in Fig. 2.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1998,
392,
42-48)
copyright 1998.
B
p50-DNA complex (upper left)24 and in the ternary Fos-Jun-AP-1
site complex (lower right)31. Lines with arrowheads, hydrogen
bonds; lines with filled circles at either end, van der Waals
contacts; solid lines, major-groove and sugar-phosphate
interactions; dashed lines, minor-groove interactions. The
coloured blocks indicate which protein is involved. c, Detailed
view (using Ribbons50) of NFAT interactions in the major groove,
showing the roles of Arg 421, Glu 427, Arg 430, Gln 571 and Arg
572 in specifying base pairs. Arg 430 is supported by salt links
to Glu 427, which also accepts hydrogen bonds from the
main-chain NH of Tyr 424 and from N4 of Cyt 2'. The view is
essentially the same as that in Fig. 2.