Figure 1.
FIG. 1. Comparison of NBD1 structures. A, sequence
alignment of human and mouse NBD1 with NBD domains from other
ABC transporters. Blue background, -strands; pink, -helices; purple, 3[10]
helices; gray, absence of density in the electron density map.
Numbering of the secondary structure elements for CFTR NBD1 is
indicated in shaded blocks in the top row. Bold blue indicates
residues with high sequence conservation in ABC domains, while
bold red indicates residues that have been mutated in forms of
hNBD1. Protein Data Bank ID codes are indicated in parentheses.
B, stereo pair of superimposed worm diagrams of NBD1 from CFTR.
Regions with conformational differences are shown in cyan for
hNBD1-2b-F508A (molecule E), blue for hNBD1-7a- F508,
and gold for mNBD1 (molecule B). Bound ATP is shown in wire
frame representation employing the same colors. The figure was
made using Spock (31).
-strands; pink, 
-helices; purple, 3[10]
helices; gray, absence of density in the electron density map.
Numbering of the secondary structure elements for CFTR NBD1 is
indicated in shaded blocks in the top row. Bold blue indicates
residues with high sequence conservation in ABC domains, while
bold red indicates residues that have been mutated in forms of
hNBD1. Protein Data Bank ID codes are indicated in parentheses.
B, stereo pair of superimposed worm diagrams of NBD1 from CFTR.
Regions with conformational differences are shown in cyan for
hNBD1-2b-F508A (molecule E), blue for hNBD1-7a- 
F508,
and gold for mNBD1 (molecule B). Bound ATP is shown in wire
frame representation employing the same colors. The figure was
made using Spock (31).