The receptor-binding site of human relaxin II. A dual prong-binding mechanism.
Recent structure/function studies on human relaxin II have led to the conclusion that the arginines B13 and/or B17 are important for biological activity. These studies have been confirmed and extended with the help of chemically synthesized derivatives, i.e. dicitrulline ( B13, B17), two monocitrulline ( B13 and B17), a dilysine ( B13, 17), and alanine ( B17) relaxins. The CD spectra of synthetic human relaxin and of the derivatives are indistinguishable. Yet, only the native human relaxin II is biologically active and binds strongly to relaxin receptor preparations in vitro. The inactivation is strictly due to side chain functions, in particular the replacement of either or both arginines in the positions B13 or B17. Binding is mediated by a two-prong electrostatic and hydrogen-binding interaction via arginines B13 and B17. Neither B13 nor B17 alone are sufficient and a positive charge equidistant from the B chain helix is equally insufficient. This binding mechanism appears to be unique, as concerns hormone receptor interaction.[1]References
- The receptor-binding site of human relaxin II. A dual prong-binding mechanism. Büllesbach, E.E., Yang, S., Schwabe, C. J. Biol. Chem. (1992) [Pubmed]
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