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Article

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

Nature communications - 3 Jan 2012

Andersen Jan Terje, Dalhus Bjørn, Cameron Jason, Daba Muluneh Bekele, Plumridge Andrew, Evans Leslie, Brennan Stephan O, Gunnarsen Kristin Støen, Bjørås Magnar, Sleep Darrell, Sandlie Inger

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22215085
DOI: 10.1038/ncomms1607
PMCID: PMC3272563

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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