|
Figure 1.
Figure 1. Homology modeling of Smg SAM domain. (a) Sequence
alignment of SAM domains of Smg homologs and selected proteins.
GenBank accession numbers are indicated on the right. Secondary
structure elements corresponding to the EphB2 SAM domain crystal
structure are indicated. Conserved hydrophobic residues, green;
acidic residues, red; basic residues, blue. Mutations in Smg or
Vts1 that perturbed SRE binding, red stars; benign mutation,
green diamond. Species abbreviations: dm, D. melanogaster; ag,
Anopheles gambiae; hs, Homo sapiens; mm, Mus musculus; ce, C.
elegans; ca, Candida albicans; sp, S. pombe; sc, S. cerevisiae;
dd, Dictyostelium discoideum. (b) Cladogram representing overall
sequence similarity and domain architecture of the Smg homologs.
See text for description of SAM, SSR1 and SSR2 domains. Zif,
CCHC zinc-finger domain (SMART43). (c,d) Ribbon and surface
representations of the Smg SAM domain, respectively. In c,
secondary structure elements encompassing RNA-binding surface
are pink and conserved side chains specific to Smg homologs are
in ball-and-stick representation. In d, regions corresponding to
conserved basic and hydrophobic residues specific to the Smg
homologs are blue and green, respectively.
|
