<unk> s vary considerably in length and design, as do peptide hormones, but their base structure is the same. They consist of one or more inactive peptide hormones or hormone chains attached to each other in a way that prevents hormone expression, often by making the chains’ binding ends inaccessible via folding and binding of other chains to said ends. For hormonal expression to be induced, the binding ends of hormones but either bind to receptors in the cell membrane, or in the case of steroids, bind to steroid receptor proteins in the cell, both of which mediate hormone expression. Proinsulin molecule; schematic, topological drawing. B chain (orange), C-peptide (gray), and A chain (green). The C-peptide is seen to bind to the B and A chains and suppress hormonal expression. When cleavage occurs to produce insulin, the B and A chain are connected by disulfide bonds, while the C-peptide is cut out and discarded. Some<unk> s contain structures other than inactive peptide hormones for the purpose of keeping hormone expression suppressed. For example, proinsulin contains an extra non-hormonal chain called C-peptide that binds two insulin peptide chains together, designed to keep both chains inactive by binding to their ends, specifically, their C-domain junctions, which have been proposed to be their site of binding to hormone-expression receptors in the cell. Despite the restrictions it enables, the C-peptide folds the proinsulin chains to make their junction ends accessible to be cleaved by<unk>  convertases later, making the folding of the proinsulin chain containing C-peptide essential for the proper cleavage of proinsulin to successfully produce insulin.
Prohormone
Xenohormone
Neurohormone
Hormone
Local hormone
Gastrointestinal hormone
Sex hormone
Neuropeptide