| Autor: |
Craig, A.Grey, Fischer, Wolfgang H, Park, Minkyu, Rivier, Jean E, Musselman, Brian D, Powell, James F.F, Reska-Skinner, Sabina M, Prakash, Manish Om, Mackie, George O, Sherwood, Nancy M |
| Zdroj: |
FEBS Letters; August 1997, Vol. 413 Issue: 2 p215-225, 11p |
| Abstrakt: |
The primary structure of two forms of gonadotropin releasing hormone (GnRH) from tunicate (Chelyosoma productum) have been determined based on mass spectrometric and chemical sequence analyses. The peptides, tunicate GnRH‐I and ‐II, contain features unprecedented in vertebrate GnRH. Tunicate GnRH‐I contains a putative salt bridge between Asp5and Lys8. A GnRH analog containing a lactam bridge between Asp5and Lys8was found to increase release of estradiol compared with that of the native tunicate GnRH‐I and ‐II. Tunicate GnRH‐II contains a cysteine residue and was isolated as a dimeric peptide. These motifs suggest that the conformation plays an important role in receptor activation. |
| Databáze: |
Supplemental Index |
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