A regulatable switch mediates self-association in an immunoglobulin fold

A native to amyloidogenic transition regulated by a backbone trigger

Formation of a stable oligomer of beta-2 microglobulin requires only transient encounter with Cu(II)

MIQRTPKIQVYSRFPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM

28% PEG 3350, 200 mM ammonium tartrate dibasic, pH 7.40, VAPOR DIFFUSION, SITTING DROP, temperature 288K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

class-1 MHC, amyloid, protein folding, dialysis-related amyloidosis, beta-2 microglobulin, Disease mutation, Glycation, Glycoprotein, Immune response, Immunoglobulin domain, MHC I, Pyrrolidone carboxylic acid, Secreted, IMMUNE SYSTEM

IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDRDM