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Figure 4.
Figure 4. Tryptophan Recognition by the U2AF^35 RRM and
U2AF^65-RRM3(A) Ribbon representation of the U2AF^35 RRM in
complex with the proline-rich region in the N terminus of
U2AF^65 (Kielkopf et al., 2001). Side chains involved in the
molecular interface are shown. Trp134, which is not conserved in
U2AF^65-RRM3, is labeled magenta.(B) Ribbon representation of
the U2AF^65-RRM3/SF1 complex. Side chains involved in tryptophan
coordination are shown.(C) Sequence alignment of noncanonical
RRMs with an extended and negatively charged helix A.
Conserved residues that mediate recognition of SF1 Trp22 and
U2AF^65 Trp92 by U2AF^65-RRM3 and the U2AF^35 RRM, respectively,
are shown in white on black. Trp134 in the U2AF^35 RRM is
colored magenta.(D) Domain organization of proteins that contain
noncanonical RRMs. The domain annotations are according to SMART
(Schultz et al., 1998). “R/S” is an arginine-serine-rich
region, “STY Kc” is a phoshokinase domain, and “Zn” are
zinc binding domains.
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