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On the Cover: Model of the structure of Btk SH2 domain. A,
A stereo view of the modeled structure of Btk SH2
domain. The analyzed XLA-causing mutations are shown on the left.
On the right are amino acids predicted to be involved in the binding
of pY-containing ligands. The peptide bound to the domain has sequence pYEEI.
Residues recognizing and binding phosphotyrosine are colored with orange,
and those binding to pY + 1 are in green. The hydrophobic pY + 3 binding
pocket is in yellow. Y334, participating in both pY + 1 and pY + 3
binding, is in white. B, Binding of the pYEEI peptide to the
Btk SH2 domain. Residues involved are colored as in A.
The SH2 domain is shown with the surface presentation, and the peptide
with a stick model. The binding residues are clearly visible. The
peptide-SH2 domain interaction indicates structural complementarity.
(Figure 1 from Mattsson, P. T., I. Lappalainen, C.-M. Backesjo, E. Brockmann,
S. Lauren, M.Vihinen, and C. I. E. Smith. Six X-linked
agammaglobulinemia-causing missense mutations in the Src homology a
domain of Bruton's tyrosine kinase: phosphotyrosine-binding and
circular dichroism analysis. J. Immunol. 164:4170.)
[Table of Contents]
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