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Figure 1.
Fig. 1. Comparison of the structures of HSA-T[4] and (a)
HSA-myristate-T[4] (b). The protein secondary structure is shown
schematically with the subdomains color-coded as follows: IA,
red; IB, light red; IIA, green; IIB, light-green; IIIA, blue;
IIIB, light blue. This color scheme is maintained throughout.
Ligands are shown in a space-filling representation, colored by
atom type: carbon (fatty acid), gray; carbon (T[4]), brown;
nitrogen, blue; oxygen, red; iodine, magenta. T[4]-binding sites
are labeled Tr1-Tr5; fatty acid-binding sites are labeled
FA1-FA7. Except where stated otherwise, molecular graphics were
prepared by using BOBSCRIPT (40) and RASTER3D (41). (c)An F[obs]
- F[calc] simulated annealing omit map (29) contoured at 3  for T[4]
bound to site Tr1 in subdomain IIA of the R218P mutant. Selected
amino acid side chains are colored by atom type. Hydrogen bonds
are indicated by dashed orange lines. (d) Schematic structure of
T[4] hormone, indicating key nomenclature.
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