Title of article :
Regulation of Chemokine Recognition by Site-Specific Tyrosine Sulfation of Receptor Peptides Original Research Article
Author/Authors :
Levi S. Simpson، نويسنده , , John Z. Zhu، نويسنده , , Theodore S. Widlanski، نويسنده , , Martin J. Stone، نويسنده ,
Issue Information :
ماهنامه با شماره پیاپی سال 2009
Pages :
9
From page :
153
To page :
161
Abstract :
Sulfation of tyrosine is a common posttranslational modification of secreted proteins that influences numerous physiological and pathological processes. Studies of tyrosine sulfation have been hindered by the difficulty of introducing sulfate groups at specific positions of peptides and proteins. Here we report a general strategy for synthesis of peptides containing sulfotyrosine at one or more specific position(s). The approach provides a substantial improvement in both yield and convenience over existing methods. Using synthetic sulfopeptides derived from the chemokine receptor CCR3, we demonstrate that sulfation enhances affinity for the chemokine eotaxin by ∼7-fold or more than 28-fold, depending on which of two adjacent tyrosine residues is sulfated. The synthetic methodology will substantially enhance efforts to understand the functional and structural consequences of protein tyrosine sulfation.
Journal title :
Chemistry and Biology
Serial Year :
2009
Journal title :
Chemistry and Biology
Record number :
1159653
Link To Document :
بازگشت