Journal article

Relaxin-like bioactivity of ovine insulin 3 (INSL3) analogues

AA Claasz, CP Bond, RA Bathgate, L Otvos, NF Dawson, RJ Summers, GW Tregear, JD Wade

European Journal of Biochemistry | BLACKWELL PUBLISHING LTD | Published : 2002

Abstract

Relaxin is an insulin-like peptide consisting of two separate chains (A and B) joined by two inter- and one intrachain disulfide bonds. Binding to its receptor requires an Arg-X-X-X-Arg-X-X-Ile motif in the B-chain. A related member of the insulin superfamily, INSL3, has a tertiary structure that is predicted to be similar to relaxin. It also possesses an Arg-X-X-X-Arg motif within its B-chain, although this is displaced by four amino acids towards the C-terminus from the corresponding position within relaxin. We have previously shown that synthetic INSL3 itself does not display relaxin-like activity although analogue (Analogue A) with an introduced arginine residue in the B-chain giving it ..

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University of Melbourne Researchers