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48 Protein folding and three-dimensional domain swapping: a strained relationship? Marcia E Newcomer Many proteins function as multimeric assemblies into which the been described. In addition, examples of swapped and folded individual promoters organize as higher order structures. unswapped versions of a protein fold shared by homologous An oligomerization mechanism that appears to impose the sequences are commonly observed. In order for a monomeric coordination of events during folding and oligomer assembly is protein to ‘swap’ structural elements, there must be a three-dimensional domain swapping. Recent studies have hinge, or linker region, that permits the protein to recapit- focused on revealing the structural basis of domain swapping ulate the native fold from two polypeptide chains and form and a possible role for domain swapping in the regulation of essentially what one might term a ‘hybrid’ fold. Eisenberg protein aggregation and activity. and co-workers [2] have defined the structure that the polypeptide adopts when monomeric as the ‘closed Addresses monomer’ and the conformation of the polypeptide in Departments of Biological Sciences and Chemistry, 202 Life Sciences the domain-swapped oligomer as the ‘open monomer’. The Building, Louisiana State University, Baton Rouge, LA 70803, USA; ‘closed interface’ is the intramolecular interface found in the e-mail: newcomer@lsu.edu monomer structure and recreated by two polypeptide Current Opinion in Structural Biology 2002, 12:48–53 chains in the domain-swapped structure. The ‘open inter-