Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel. Chapter

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.

authors

• Huang, Yun
• Ma, Guolin

altmetric score

• 1.5

author list (cited authors)

• Ma, G., He, L., Jing, J. i., Tan, P., Huang, Y., & Zhou, Y.

citation count

• 1

complete list of authors

• Ma, Guolin||He, Lian||Jing, Ji||Tan, Peng||Huang, Yun||Zhou, Yubin

Book Title

• CRAC CHANNEL: METHODS AND PROTOCOLS

publication date

• January 2018

publisher

• Springer Nature  Publisher

published in

• Methods in molecular biology (Clifton, N.J.)  Journal

keywords

• Calcium
• Calcium Release Activated Calcium Channels
• Calcium Release-activated Calcium Channel
• Calcium Signaling
• Cloning, Molecular
• Cross-linking
• Cysteine
• Disulfide Bond
• Gene Expression
• Genetic Engineering
• HEK293 Cells
• Humans
• Ion Channel Gating
• Lymphocyte Activation
• Membrane Protein
• Mutagenesis, Site-Directed
• Orai1
• Plasmids
• Protein Multimerization
• Store-operated Calcium Entry
• Stromal Interaction Molecule
• Structure
• Structure-Activity Relationship

PubMed Central ID

• 30203285

Digital Object Identifier (DOI)

• 10.1007/978-1-4939-8704-7_13

International Standard Book Number (ISBN) 13

• 978-1-4939-8702-3

start page

• 147

end page

• 166

volume

• 1843

URL

• http://dx.doi.org/10.1007/978-1-4939-8704-7_13