|
Figure 6.
Fig. 6. Key residues required for elonginBC binding. An Ala
scan of the SOCS3 SOCS box to determine residues required for
elonginBC binding was performed. Co-expression of 12 SOCS box
domain constructs, each containing a single Ala mutation, with
elonginBC was performed in E. coli, and glutathione Sepharose
was used to pull down GST-labelled proteins present in the cell
lysate. (a) The following mutations completely interfered with
elonginBC binding: Val1, Thr3, Leu4, Leu7, Cys8, Arg9 and Val12.
Of these, only the L4A mutation completely abolished binding.
(c) Residues identified by Ala scan are highlighted on a surface
representation of elonginBC where hydrophobic residues on the
surface of elonginC are shown in yellow. The BC box of SOCS3
(red) is shown in cartoon representation with important side
chains displayed in “stick” representation. ElonginC is
shown in blue and elonginB in green.
|
