Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel. | Chapter individual record
abstract

ORAI1 constitutes the pore-forming subunit of the calcium release-activated calcium (CRAC) channel, a prototypical store-operated channel that is essential for the activation of cells of the immune system. Here we describe a convenient yet powerful cross-linking approach to examine the pore architecture of CRAC channels using ORAI1 proteins engineered to contain one or two cysteine residues. The generalizable cross-linking in situ approach can also be readily extended to study other integral membrane proteins expressed in various types of cells.

book title

The CRAC Channel

authors
author list (cited authors)
Ma, G., He, L., Jing, J. i., Tan, P., Huang, Y., & Zhou, Y.
publication date
2018
publisher
keywords
  • Structure
  • Humans
  • Stromal Interaction Molecule
  • Calcium Release-activated Calcium Channel
  • Store-operated Calcium Entry
  • Protein Multimerization
  • Orai1
  • Mutagenesis, Site-Directed
  • Calcium Release Activated Calcium Channels
  • HEK293 Cells
  • Structure-Activity Relationship
  • Disulfide Bond
  • Genetic Engineering
  • Calcium Signaling
  • Cloning, Molecular
  • Plasmids
  • Cysteine
  • Lymphocyte Activation
  • Ion Channel Gating
  • Cross-linking
  • Gene Expression
  • Membrane Protein
  • Calcium
altmetric score

1.5

citation count

0

PubMed ID
30203285
identifier
380807SE
Digital Object Identifier (DOI)
International Standard Book Number (ISBN) 13
9781493987023
start page
147
end page
166
volume
1843