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PMID:8216305
| Citation |
Büllesbach, EE and Schwabe, C (1993) Mouse relaxin: synthesis and biological activity of the first relaxin with an unusual crosslinking pattern. Biochem. Biophys. Res. Commun. 196:311-9 |
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| Abstract |
According to a recently published cDNA sequence, mouse relaxin has an extra amino acid in the C-terminal end of the A chain and thus an interchain loop consisting of 25 amino acids instead of the usual 24-membered ring. Because of the restrictive disulfide link arrangement the extra residue can be expected to cause a loop out in the C-terminal alpha-helix. We have chemically synthesized authentic mouse relaxin as well as an analog without the additional A chain residue and found that the native hormone, although active, was inferior to its insulin-like analog. This result is in harmony with our previous study which suggests that the surface of relaxin represented by the C-terminal helix of the A chain is positioned opposite to the surface that contains the receptor interaction site and therefore is less sensitive to modifications. |
| Links |
PubMed Online version:10.1006/bbrc.1993.2250 |
| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Animals; Biological Assay; Brain/metabolism; Circular Dichroism; Disulfides/chemistry; Mice; Molecular Sequence Data; Protein Structure, Secondary; Receptors, G-Protein-Coupled; Receptors, Peptide/metabolism; Relaxin/analogs & derivatives; Relaxin/chemistry; Relaxin/pharmacology; Sequence Homology, Amino Acid |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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