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1. GH-receptor complex. (From Fuh et aI. 1992) tryptophan residue with opposite sides of the 4 antiparallel a helixes in the hormone. A second more carboxy terminal P barrel domain interacts with its adjacent partner in the hormone-(receptorh complex to stabilize the trimeric complex. DeVos et al. (1992) suggest that receptor dimerization constitutes the signal for growth (Fig. 1). Mutational Analysis of Receptor Residues Important for Hormone Binding One of the features of the Genentech crystallographic structure is the involvement of hormone binding elements either within or adjacent to the universally conserved first two disulphide loops (Fuh et al.
Examination of the crystallographic model shows that Glu-33 of hGH is situated 7 A from Glu-127 of the receptor, and sits adjacent Glu-33, facing receptor Glu-127. 7 A we had predicted by application of electrostatic theory to the Ca2 + dependence characteristics (Barnard et al. 1989). We therefore conclude that the carboxy terminus of GH helix 1 does interact with the receptor, and accounts for a large part of the Ca2 + dependence of hGH binding. Omission of this element from the Genentech map was a result of the initial homolog exchange strategy which distinguished binding elements different between ovine and human GHs and prolactins, rather than common elements in these structurally related hormones.
By Northern blot analysis. The gene was expressed in pancreas and in GI tract with the highest level of expression in the terminal ileum. 5 mg GHRH) to adult male rats for 15 days. Peptide 23 gene expression was found to be positively regulated by GHRH in pancreas, duodenum, jejunum and cecum, adrenal glands and heart. Although peptide 23 initially was found to be secreted by rat pituitary cells in culture, the gut appears to be the main site of its gene expression in intact animals. Peptide 23 appears to be a member of a multi-gene family which includes reg and pancreatic thread protein (unpublished observations).