title: Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain.
abstract: Oligomerization by 3D domain swapping is found in a variety of proteins of diverse size, fold and function. In the early 1960s this phenomenon was postulated for the oligomers of ribonuclease A, but it was not until the 1990s that X-ray diffraction provided the first experimental evidence of this special manner of oligomerization. Nowadays, structural information has allowed the identification of these swapped oligomers in over one hundred proteins. Although the functional relevance of this phenomenon is not clear, this alternative folding of protomers into intertwined oligomers has been related to amyloid formation. Studies on proteins that develop 3D domain swapping might provide some clues on the early stages of amyloid formation. The SH3 domain is a small modular domain that has been used as a model to study the basis of protein folding. Among SH3 domains, the c-Src-SH3 domain emerges as a helpful model to study 3D domain swapping and amyloid formation.
authors.affiliation: Department of Chemistry and Physics, University of Almería, Agrifood Campus of International Excellence (ceiA3), Research Centre for Agricultural and Food Biotechnology (BITAL), Carretera de Sacramento s/n, Almería 04120, Spain. Electronic address: acamara@ual.es.
authors.forename: Ana
authors.initials: A
authors.lastname: Cámara-Artigas
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure*; D001665:Binding Sites; D003198:Computer Simulation; D003461:Crystallography / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D000072417:Protein Domains; D017510:Protein Folding; D018909:src Homology Domains
chemical_list: D000682:Amyloid
keywords: 3D domain swapping; Amyloid; Intertwined dimer; Protein folding; SH3 domain; X-ray crystallography