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Relaxin has conformational homology with insulin

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Abstract

RELAXIN, a polypeptide hormone synthesised and stored in the corpus luteum, is responsible for the dilation of the symphysis pubis in most mammals before parturition. Porcine relaxin (molecular weight ∼5,600) consists of one A chain and one B chain linked by disulphide bonds. The amino acid sequence of the two chains is consistent with interchain and intrachain disulphide crosslinks of the same disposition as those of insulin1,2. Although only five further residues are identical to those in equivalent positions of porcine insulin, the model presented here shows that relaxin may have a tertiary structure closely resembling that of insulin. The residues of the hydrophobic core of relaxin differ from those of insulin but are close packed and occupy the same volume.

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Authors and Affiliations

  1. Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1, UK

    S. BEDARKAR, W. G. TURNELL & T. L. BLUNDELL

  2. Department of Biochemistry, Medical University of South Carolina, Charleston, South Carolina, 29401

    C. SCHWABE

Authors
  1. S. BEDARKAR
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  2. W. G. TURNELL
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  3. T. L. BLUNDELL
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  4. C. SCHWABE
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BEDARKAR, S., TURNELL, W., BLUNDELL, T. et al. Relaxin has conformational homology with insulin. Nature 270, 449–451 (1977). https://doi.org/10.1038/270449a0

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  • DOI: https://doi.org/10.1038/270449a0

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