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Figure 1.
Figure 1. Structure of the Ligand-Free Src TEF1W Mutant(a)
Structure of the unliganded form of TEF1W Src SH2 showing the
phosphate group and the residues interacting with TrpEF1. The
secondary structure nomenclature indicated follows [8], which
names the secondary structural elements sequentially, αA, βB,
βC, etc., loops being named for the two secondary structural
elements they connect, and residues then being designated by the
sequential position they occupy on that secondary structural
element. For the residues of the phosphotyrosylated peptide, pY
0 indicates the phosphotyrosine, and pY +n and pY-n designate
residues n amino acids C- and N-terminal to it, respectively. It
should be noted that packing interactions stabilize much of the
BC loop in β strand conformation, but these residues are still
shown as loop so as to facilitate comparison with other SH2
domains. Residues discussed in the text are displayed and
labeled.(b) Stereo diagram of the σ[A] weighted 2F[obs] −
F[c] electron density map for the unliganded TEF1W Src SH2
showing TrpEF1 and the phosphate group. Density is contoured at
1.0 σ. The figure is in approximately the same orientation as
in (a).
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