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Figure 2.
Interactions of the phosphorylation site in nonphosphopeptide
and phosphopeptide HLA A2 complexes. Accommodation of the
phosphate moiety by HLA A2 is accompanied by changed
interactions in the complex, adding to the differential
presentation of altered self. Stick representation of peptides
and of heavy-chain side chains that interact with the
phosphorylation site. Yellow indicates nonphospho-pHLA A2
complexes. Green indicates phospho-pHLA A2 complexes. (A–C)
Phosphorylation of P5-Ser in CDC25b leads to an altered peptide
conformation attributable to steric constraints. (D–F)
Phosphorylation of P4-Ser in IRS2 gives rise to numerous
interactions and subtly alters the conformation of Arg 65 and
Lys 66. (G–I) Phosphorylation of P4-Ser in β-catenin
stabilizes the mobile peptide residues P3 to P6.
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