Cysteines in CH1 underlie retention of unassembled Ig heavy chains.

doi:10.1074/jbc.M500161200

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Article

Cysteines in CH1 underlie retention of unassembled Ig heavy chains.

The Journal of biological chemistry - 15 Apr 2005

Elkabetz Yechiel, Argon Yair, Bar-Nun Shoshana

Abstract excerpt

Conformation, structure, and oligomeric state of immunoglobulins not only control quality and functional properties of antibodies but are also critical for immunoglobulins secretion. Unassembled immunoglobulin heavy chains are retained intracellularly by delayed folding of the C(H)1 domain and irreversible interaction of BiP with this domain. Here we show that the three C(H)1 cysteines play a central role in...

Topics

Amino Acid Sequence
Animals
COS Cells
Cysteine
DNA Primers
Disulfides
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum Chaperone BiP
Glycoside Hydrolases
Heat-Shock Proteins
Immunoglobulin Heavy Chains

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Immunoglobulin Light Chains

Immunoprecipitation

Mice

Models, Biological

Molecular Chaperones

Molecular Sequence Data

Mutation

Source

Open in PubMed

Identifiers

PMID: 15705573
DOI: 10.1074/jbc.M500161200

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