Sequence of two gonadotropin releasing hormones from tunicate suggest an important role of conformation in receptor activation

FEBS Letters

Rivier, Jean E³  Mackie, George O¹  Prakash, Manish Om¹  Craig, A.Grey³  Musselman, Brian D²  Park, Minkyu³  Powell, James F.F¹  Reska-Skinner, Sabina M¹  Sherwood, Nancy M¹  Fischer, Wolfgang H³ 

[1] Department of Biology, University of Victoria, Victoria, B.C. V8W 2Y2, Canada;Perceptive Biosystems Inc., Framingham, MA 01701, USA;The Clayton Foundation, Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA

关键词: Gonadotropin releasing hormone;    Saltbridge;    Disulfide bridge;    Lactam bridge;    Mass spectrometry;    Chemical sequencing;    DTT;    dithiothreitol;    GnRH;    gonadotropin releasing hormone;    tunGnRH;    tunicate GnRH;    HPLC;    high performance liquid chromatography;    MALD;    matrix assisted laser desorption;    MS;    mass spectrometry;    PSD;    post source decay;    TCEP;    tris(2-carboxyethyl)phosphine;    TOF;    time of flight;   

DOI  :  10.1016/S0014-5793(97)00840-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Asp⁵ and Lys⁸. A GnRH analog containing a lactam bridge between Asp⁵ and Lys⁸ was 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.

【 授权许可】

Unknown