Building protein structure and function from modular units

Many proteins in multicellular organisms are made from combinations of several, clearly identifiable, autonomously folding domains or modules. The structures of many of the constituent modules and some module pairs are now known. This review briefly describes some of the recent X-ray crystallographic and nuclear magnetic resonance (NMR) structural work on modules 'dissected' from proteins that are often large, membrane-bound and glycosylated. These include important proteins involved in cell adhesion, clotting, fibrinolysis and signalling. The structure and function of the intact proteins is discussed in the light of the recent structural work.