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A SURVEY OF X‐RAY DIFFRACTION STUDIES OF ENZYME‐OTHER MOLECULE INTERACTIONS AS POSSIBLE MODELS FOR RECEPTOR SITES *
Author(s) -
Lipscomb William N.
Publication year - 1981
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1981.tb50576.x
Subject(s) - molecule , diffraction , chemistry , crystallography , biophysics , physics , biology , optics , organic chemistry
In the absence of a structure for a hormone-receptor complex, one may ask what systems of known structure are most likely to provide information about hormone interactions. Here, I discussed enzyme-substrate, enzyme-(protein) inhibitor, enzyme fragment (S peptide), and antibody-hapten (or antigen) interactions as possible models. Following a study of a fairly inflexible hormone (insulin) and of a flexible hormone (glucagon), I commented on probable binding regions. Finally, my conclusion was that, at present, allosteric enzymes have many of the characteristics thought to be present in those hormone-receptor interactions which activate enzymes. This model does not necessarily apply in detail to examples of hormone interactions that affect permeability of the cell wall or activate genetic processes.