Characterisation of the single copy trefoil peptides intestinal trefoil factor and pS2 and their ability to form covalent dimers

FEBS Letters

Bates, Paul A.²  Freemont, Paul S.³  Chinery, Rebecca¹  De, Amitabha³ 

[1] Department of Pharmacology, The Royal College of Surgeons of England, 35-43 Lincoln's Inn Fields, London WC2A 3PN, UK;Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, P.O. Box 123, Lincoln's Inn Fields, London WC2A 3PX, UK;Protein Structure Laboratory, Imperial Cancer Research Fund, P.O. Box 123, Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: Trefoil peptide;    Protein modelling;   

DOI  :  10.1016/0014-5793(94)01297-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A bacterial recombinant expression system was established to produce biologically active rat Intestinal Trefoil factor (rITF). Characterisation of purified rITF shows that both monomers and dimers can be observed under reducing and non-reducing conditions, respectively. Site-directed mutagenesis studies show that Cys57 is necessary for rITF dimer formation. Samples of human gastrointestinal tissue following biopsy also demonstrated the presence of reducible human pS2 and ITF covalent dimers. Three-dimensional models for pS2 and ITF support the hypothesis that both pS2 and ITF can exist as disulphide-linked dimers in vivo and that any proposed function for these peptides must take dimer formation into account.

【 授权许可】

Unknown