Prediction of tyrosine sulfation in seven-transmembrane peptide receptors
| Autor: | Justin Liu, Ryan H. Moy, Hugh B. Nicholas, Kristine M. Yu, Henry C. Lin, Grace L. Rosenquist |
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| Rok vydání: | 2002 |
| Předmět: |
Tyrosine sulfation
Receptors Peptide Endocrinology Diabetes and Metabolism Biology Receptors Corticotropin-Releasing Hormone Receptor tyrosine kinase Glucagon-Like Peptide-1 Receptor Protein Structure Secondary Endocrinology Protein structure Sulfation Receptors Glucagon Animals Humans Amino Acid Sequence Tyrosine Receptors Immunologic Receptor Peptide sequence Conserved Sequence G protein-coupled receptor Binding Sites Sulfates Receptors LH Receptors Formyl Peptide Biochemistry biology.protein Receptors FSH |
| Zdroj: | Endocrine. 19(3) |
| ISSN: | 1355-008X |
| Popis: | Posttranslational modification by tyrosine sulfation regulates many important protein-protein interactions and modulates the binding affinity and specificity of seven-transmembrane peptide receptors. We developed a log-odds position-specific-scoring-matrix (PSSM) to accurately predict tyrosine sulfation using 62 tyrosine sites known to be sulfated and 421 tyrosine sites known not to be sulfated. We predict that 49 tyrosines of 32 seven-transmembrane peptide receptors are sulfated. Although we did not incorporate characteristics of confirmed sulfation sites such as clustering and conservation across species into our PSSM, our predicted sites nevertheless exhibited these characteristics. The observed conservation suggests that there are strong evolutionary pressures to preserve selected biological activity of seven-transmembrane receptors. The predicted tyrosine sulfation sites predominantly occur in the extracellular tail and extracellular loop 2, regions consistent with their association with binding pockets of the receptor. |
| Databáze: | OpenAIRE |
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