The peptide hormone, angiotensin II, acts primarily via type I (AT(1)) and type II (AT(2)) angiotensin receptors. Proteolytic fragments of angiotensin II also have biological activity via these and other receptors, with actions that may mimic or antagonise angiotensin II. Most notably, a high affinity-binding site for angiotensin IV (the Val(3)-Phe(8) fragment of angiotensin II) has recently been identified as the insulin-regulated aminopeptidase (IRAP). While AT(1) and AT(2) receptors are seven transmembrane-spanning, G protein-coupled receptors with some well-established features of relevance to health and disease, the existence of separate receptor systems for angiotensin fragments offers exciting possibilities for new therapeutics to target the diverse actions of the angiotensin peptides.