Mapping receptor–ligand interactions with synthetic peptide arrays: Exploring the structure and function of membrane receptors

2012 ◽  
Vol 91 (4) ◽  
pp. 349-356 ◽  
Author(s):  
Rudolf Volkmer ◽  
Ines Kretzschmar ◽  
Victor Tapia
1976 ◽  
Vol 70 (2) ◽  
pp. 261-286 ◽  
Author(s):  
C R Kahn

Receptors for peptide hormones and neurotransmitters are integral components of the plasma membrane of cells which serve to couple the external milieu to the intracellular regulators of metabolism. These macromolecules are usually high molecular weight glycoproteins, and in many cases appear to have more than one subunit capable of binding the hormone. The interaction of the hormone or neurotransmitter with its receptor is rapid, reversible, and of high affinity and specificity. Many receptors exhibit cooperative properties in hormone binding or biological function. The concentration of receptors on the membrane is a function of continued synthesis and degradation, and may be altered by a variety of factors including the hormone itself. The fluid mosaic nature of the membrane may allow hormone receptors and effectors to exist in free floating states. Further investigations of the hormone-receptor interaction will no doubt yield new insights into both the mechanism of hormone action and membrane structure and function.


Author(s):  
Henriks Zenkevičs ◽  
Ilze Vosekalna ◽  
Vija Vose

Role of Carboxyl Groups in the Secondary Structure and Function of Sturgeon Gonadotropin Free negatively charged carboxyl groups were selectively modified (neutralised) in sturgeon (Acipenser güldenstädti Br.) gonadotropic hormone (GTH) α and β subunits. Eleven free carboxyl groups, three in the α and eight in the β subunit, were neutralised by reaction with glycine ethyl ester. Investigation of reassociated α-β dimers (recombinants) comprising one or both modified subunits showed that specific hormonal activity was completely lost while immunoreactivity was lowered in comparison with that of the standard α-β dimer. CD-spectroscopy of the modified subunits did not indicate any considerable changes in their spatial structure. A conclusion was made that free COOH groups of GTH were important as bearers of the negative charge necessary for the hormone activity on the level of the hormone-specific membrane receptors.


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