Figure 2.
Fig. 2. Comparison of the bound configurations of T[4] in
HSA. (a) Site Tr1 in subdomain IIA. There is only very weak
electron density for the side chain of R218 because variation in
the position of this residue and atoms beyond C were
omitted from the refined model; the position shown in the figure
is indicative only but is consistent with the location of the
main-chain atoms and steric constraints imposed by neighboring
residues and the T[4] ligand. (b) Site Tr2 in subdomain IIIA.
(c) Sites Tr3 and Tr4 in subdomain IIIB (from the R218H mutant
structure, because this model shows the least disorder of the
C-terminal helix). (d) Site Tr5 in the interdomain cleft of the
HSA-myristate complex. Figures were prepared by using MOLSCRIPT
(41) and PYMOL (42). Selected amino acid side chains are shown
colored by atom type. The van der Waals surface of the ligand is
represented by a semitransparent magenta surface. Hydrogen bonds
are indicated by dashed orange lines.
were
omitted from the refined model; the position shown in the figure
is indicative only but is consistent with the location of the
main-chain atoms and steric constraints imposed by neighboring
residues and the T[4] ligand. (b) Site Tr2 in subdomain IIIA.
(c) Sites Tr3 and Tr4 in subdomain IIIB (from the R218H mutant
structure, because this model shows the least disorder of the
C-terminal helix). (d) Site Tr5 in the interdomain cleft of the
HSA-myristate complex. Figures were prepared by using MOLSCRIPT
(41) and PYMOL (42). Selected amino acid side chains are shown
colored by atom type. The van der Waals surface of the ligand is
represented by a semitransparent magenta surface. Hydrogen bonds
are indicated by dashed orange lines.