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The carboxy‐terminal domain of the receptor‐associated protein binds to the Vps10p domain of sortilin
Author(s) -
Tauris Jacob,
Ellgaard Lars,
Jacobsen Christian,
Nielsen Morten S,
Madsen Peder,
Thøgersen Hans C,
Gliemann Jørgen,
Petersen Claus Munck,
Moestrup Søren K
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00559-6
Subject(s) - receptor , binding domain , n terminus , plasma protein binding , c terminus , binding site , chemistry , ldl receptor , microbiology and biotechnology , biochemistry , biology , peptide sequence , amino acid , lipoprotein , gene , cholesterol
Binding of the receptor‐associated protein (RAP) to the newly identified putative sorting receptor, sortilin, was analyzed by surface plasmon resonance analysis of recombinant RAP and sortilin domains and compared with binding to megalin and low density lipoprotein receptor‐related protein (LRP). The data show that the RAP‐binding site in sortilin is localized in the cysteine‐rich lumenal part homologous to yeast vacuolar protein‐sorting 10 protein (Vps10p), and the sortilin‐binding site in RAP is localized in the carboxy‐terminal domain III of the three homologous domains in RAP. Whereas sortilin bound only RAP domain III, megalin and LRP bound all RAP domains with the functional affinity order: domain III>domain I>domain II.