Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation.

@article{Chen2001StoichiometryOC,
  title={Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation.},
  author={C B Chen and Russell Wallis},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 28},
  pages={25894-902}
}
Serum mannose-binding protein (MBP) initiates the lectin branch of the complement cascade by binding to sugars on the surfaces of microorganisms and activating two MBP-associated serine proteases (MASP-1 and MASP-2). Rat serum MBP consists of oligomers containing up to four copies of a subunit that is composed of three identical polypeptide chains. Biophysical analysis of intact and truncated MASPs indicates that each MASP is a homodimer that is stabilized through interactions involving an N… CONTINUE READING

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