title: Folding of the voltage-gated K+ channel T1 recognition domain.
abstract: Voltage-gated K(+) channels (Kv) are tetramers whose assembly is coordinated in part by a conserved T1 recognition domain. Although T1 achieves its quaternary structure in the ER, nothing is known about its acquisition of tertiary structure. We developed a new folding assay that relies on intramolecular cross-linking of pairs of cysteines engineered at the folded T1 monomer interface. Using this assay, we show directly that the T1 domain is largely folded while the Kv protein is still attached to membrane-bound ribosomes. The ER membrane facilitates both folding and oligomerization of Kv proteins. We show that folding and oligomerization assays can be used to study coupling between these two biogenic events and diagnose defects in assembly of Kv channels.
authors.affiliation: Department of Physiology, University of Pennsylvania, Philadelphia 19104-6085, USA.
authors.forename: Andrey
authors.initials: A
authors.lastname: Kosolapov
authors.forename: Carol
authors.initials: C
authors.lastname: Deutsch
mesh_terms: D000818:Animals; D001704:Biopolymers; D005260:Female; D015640:Ion Channel Gating; D015221:Potassium Channels / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014982:Xenopus laevis
chemical_list: D001704:Biopolymers; D015221:Potassium Channels