Crystal Structure of an HSA/FcRn Complex Reveals Recycling by Competitive Mimicry of HSA Ligands at a pH-Dependent Hydrophobic Interface

Crystal Structure of an HSA/FcRn Complex Reveals Recycling by Competitive Mimicry of HSA Ligands at a pH-Dependent Hydrophobic Interface

The long circulating half-life of serum albumin, the most abundant protein in mammalian plasma, derives from pH-dependent endosomal salvage from degradation, mediated by the neonatal Fc receptor (FcRn). Using yeast display, we identified human serum albumin (HSA) variants with increased affinity for...

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Bibliographic Details
Main Authors: Schmidt, Michael M., Townson, Sharon A., Andreucci, Amy J., King, Bracken Matheny, Schirmer, Emily B., Murillo, Alec J., Dombrowski, Christian, Tisdale, Alison W., Lowden, Patricia A., Masci, Allyson L., Kovalchin, Joseph T., Erbe, David V., Wittrup, Karl Dane, Furfine, Eric S., Barnes, Thomas M.
Other Authors: Massachusetts Institute of Technology. Department of Biological Engineering
Format: Article
Language:en_US
Published: Elsevier B.V. 2014
Online Access:http://hdl.handle.net/1721.1/91612
https://orcid.org/0000-0003-2398-5896

Internet

http://hdl.handle.net/1721.1/91612
https://orcid.org/0000-0003-2398-5896

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