BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly.

@article{Lee1999BiPAI,
  title={BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly.},
  author={Youngsoo Lee and Joseph W. Brewer and Rachel Hellman and Linda M Hendershot},
  journal={Molecular biology of the cell},
  year={1999},
  volume={10 7},
  pages={
          2209-19
        }
}
The immunoglobulin (Ig) molecule is composed of two identical heavy chains and two identical light chains (H2L2). Transport of this heteromeric complex is dependent on the correct assembly of the component parts, which is controlled, in part, by the association of incompletely assembled Ig heavy chains with the endoplasmic reticulum (ER) chaperone, BiP. Although other heavy chain-constant domains interact transiently with BiP, in the absence of light chain synthesis, BiP binds stably to the… CONTINUE READING
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