Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor

@inproceedings{Andersen2012StructurebasedMR,
  title={Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor},
  author={Jan Andersen and Bj{\o}rn Dalhus and Jason M Cameron and Muluneh Bekele Daba and Andrew Plumridge and Leslie E. Evans and Stephan O. Brennan and Kristin St{\o}en Gunnarsen and Magnar Bj{\o}r{\aa}s and Darrell Sleep and Inger Sandlie},
  booktitle={Nature communications},
  year={2012}
}
Albumin is the most abundant protein in blood where it has a pivotal role as a transporter of fatty acids and drugs. Like IgG, albumin has long serum half-life, protected from degradation by pH-dependent recycling mediated by interaction with the neonatal Fc receptor, FcRn. Although the FcRn interaction with IgG is well characterized at the atomic level, its interaction with albumin is not. Here we present structure-based modelling of the FcRn-albumin complex, supported by binding analysis of… CONTINUE READING
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