Idioma:

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

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

Nature communications, 2012-01, Vol.3 (1), p.610-610, Article 610 [Periódico revisado por pares]

England: Nature Publishing Group

Texto completo disponível

Citações Citado por

Enviar para

Título:
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor
Autor: 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
Assuntos: Albumins - chemistry ; Binding Sites ; Escherichia coli - metabolism ; Histidine - chemistry ; Histocompatibility Antigens Class I - chemistry ; Histocompatibility Antigens Class I - genetics ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G - chemistry ; Ions ; Models, Molecular ; Molecular Conformation ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutation ; Protein Structure, Tertiary ; Receptors, Fc - chemistry ; Receptors, Fc - genetics ; Serum Albumin - chemistry ; Time Factors
É parte de: Nature communications, 2012-01, Vol.3 (1), p.610-610, Article 610
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
Descrição: 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 site-specific mutants, providing mechanistic evidence for the presence of pH-sensitive ionic networks at the interaction interface. These networks involve conserved histidines in both FcRn and albumin domain III. Histidines also contribute to intramolecular interactions that stabilize the otherwise flexible loops at both the interacting surfaces. Molecular details of the FcRn-albumin complex may guide the development of novel albumin variants with altered serum half-life as carriers of drugs.
Editor: England: Nature Publishing Group
Idioma: Inglês;Norueguês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

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

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

England: Nature Publishing Group

Buscando em bases de dados remotas. Favor aguardar.