Protein folding and three-dimensional domain swapping: a strained relationship?
Many proteins function as multimeric assemblies into which the folded individual promoters organize as higher order structures. An oligomerization mechanism that appears to impose the coordination of events during folding and oligomer assembly is three-dimensional domain swapping. Recent studies have focused on revealing the structural basis of domain swapping and a possible role for domain swapping in the regulation of protein aggregation and activity.
Newcomer
Marcia E
ME
Departments of Biological Sciences and Chemistry, 202 Life Sciences Building, Louisiana State University, Baton Rouge, LA 70803, USA. newcomer@lsu.edu
D016229:Amyloid beta-Peptides / Q000737:chemistry; D020134:Catalytic Domain / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology*
D016229:Amyloid beta-Peptides