| Autor: |
John D. Wade, Kathryn J. Smith, Antonia A. Claasz, Ping Fu, Andrew B. Clippingdale, Marc N. Mathieu, Geoffrey W. Tregear, Nicola F. Dawson |
| Rok vydání: |
2001 |
| Předmět: |
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| Zdroj: |
Relaxin 2000 ISBN: 9789048158454 |
| DOI: |
10.1007/978-94-017-2877-5_35 |
| Popis: |
Knowledge of the chemistry of relaxin has increased steadily since the first determination of its primary structure in the early 1970s. The two peptide chain/three disulfide bonds structure mirrors that of insulin and established the concept of the so-called insulin superfamily of peptides and indicated that insulin and relaxin both evolved from a common ancestral gene [1]. Advances in molecular biology and protein microisolation techniques have since led to the identification of more than six other protein members of this superfamily (Table 1). All possess the same insulin/relaxin cystine pairing pattern of one A-chain intramolecular bond and two intermolecular bonds. It is probable that with the recent completion of sequencing of the human genome several more insulin-like proteins will be identified. Indeed, a recent genomic analysis of the nematode, Caenorhabditis elegans, suggested the presence of at least ten insulin-like proteins, three of which are predicted to contain an additional disulfide bond or an A-chain intramolecular bond that is substituted by a hydrophobic interaction [2]. Like insulin, relaxin and the other members of this family are synthesized on the ribosome as preprohormones in which the A- and B-chains are joined together via a connecting C-peptide that is proteolytically removed following peptide folding [3]. The exceptions, insulin-like growth factors I and II, do not have excised C-peptides. It is of considerable interest that at a length of approximately 100 residues, the relaxin C-peptide is far longer than thought necessary for efficient folding and suggests that it might be a precursor to smaller, biologically active peptides. Indeed, recent findings have shown that insulin C-peptide plays a role in a broad range of biological activities [4]. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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