
Structural heterogeneity of membrane receptors and GTP‐binding proteins and its functional consequences for signal transduction
Author(s) -
BOEGE Fritz,
NEUMANN Eberhard,
HELMREICH Ernst J. M.
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16085.x
Subject(s) - allosteric regulation , signal transduction , receptor , microbiology and biotechnology , biology , g protein coupled receptor , g protein , computational biology , biochemistry
Recent information obtained, mainly by recombinant cDNA technology, on structural heterogeneity of hormone and transmitter receptors, of GTP‐binding proteins (G‐proteins) and, especially, of G‐protein‐linked receptors is reviewed and the implications of structural heterogeneity for diversity of hormone and transmitter actions is discussed. For the future, three‐dimensional structural analysis of membrane proteins participating in signal transmission and transduction pathways is needed in order to understand the molecular basis of allosteric regulatory mechanisms governing the interactions between these proteins including hysteretic properties and cell‐cybernetic aspects.