Ontology highlight
ABSTRACT:
SUBMITTER: Feige MJ
PROVIDER: S-EPMC2908990 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Feige Matthias J MJ Groscurth Sandra S Marcinowski Moritz M Shimizu Yuichiro Y Kessler Horst H Hendershot Linda M LM Buchner Johannes J
Molecular cell 20090601 5
A prerequisite for antibody secretion and function is their assembly into a defined quaternary structure, composed of two heavy and two light chains for IgG. Unassembled heavy chains are actively retained in the endoplasmic reticulum (ER). Here, we show that the C(H)1 domain of the heavy chain is intrinsically disordered in vitro, which sets it apart from other antibody domains. It folds only upon interaction with the light-chain C(L) domain. Structure formation proceeds via a trapped intermedia ...[more]