|
Figure 4.
Figure 4. Comparison of the CBP20 RNP Domain with PABP and
Sxl(A) CBP20 RNP domain (residues 38–118, green). The trypsin
cut between Lys-77 and Cys-81 is represented with a green dashed
line. The observed conformation of the peptide 72–77, which is
stabilized by a salt bridge between residues Lys-75 and Asp-116
and certain side chains are shown in gold. A presumed
native-like conformation of the loop 72–81 and conformations
of Tyr-43 and Phe-83, modeled from the PABP structure shown in
(B), are depicted in blue.(B) The N-terminal domain of poly (A)
binding protein (residues 11–94, red) complexed with poly (A)
(gray backbone, cyan bases). The three aromatic residues from
RNP1 (Tyr-54 and Tyr-56) and RNP2 (Tyr-14) are shown in blue.(C)
The second RNP domain of Sxl (residues 206–289, yellow) in
complex with cognate RNA. Color scheme as in (B)
|
