Mutational analysis of a lactogenic hormone reveals a role for lactogen-specific amino acid residues in receptor binding and mitogenic activity.
Mutant forms of mouse placental lactogen-II (PL-II) have been generated to assess the role of specific amino acid residues and protein regions in binding to the PRL receptor and in mitogenic activity. Conversion of any of three lactogen-specific residues significantly reduced both of these hormone functions; mutation of the two other lactogen-specific amino acids revealed only minimal effects unless these changes were coupled with a second mutation. Deletions within the PL-II protein all resulted in a complete loss of function, but switching regions between PL-II and proliferin, another member of the prolactin family in the mouse, did yield a chimeric protein with some PRL-like activity. This activity was increased substantially by conversion of one amino acid residue in the proliferin region to the corresponding lactogen-specific residue. The locations of the amino acids that have been found to affect hormone function are predicted to be closely apposed in the folded protein, suggesting that this region may be the site of interaction of this lactogenic hormone with the PRL receptor.[1]References
- Mutational analysis of a lactogenic hormone reveals a role for lactogen-specific amino acid residues in receptor binding and mitogenic activity. Davis, J.A., Linzer, D.I. Mol. Endocrinol. (1989) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
