ArticleProceedings of the National Academy of Sciences of the United States of America1997
The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 42 citations in OpenAlex.
- Evaluating the evolutionary relationship of TATA binding protein (TBP) with various folding patterns of protein domains using support vector machine (SVM).Scientific reports · 2026Article
- High Affinity Binding of the Receptor-associated Protein D1D2 Domains with the Low Density Lipoprotein Receptor-related Protein (LRP1) Involves Bivalent Complex Formation: CRITICAL ROLES OF LYSINES 60 AND 191.The Journal of biological chemistry · 2016Article
- Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake.The Journal of biological chemistry · 2009Article
- LDL receptor-related protein 1: unique tissue-specific functions revealed by selective gene knockout studies.Physiological reviews · 2008Review
- The structure of receptor-associated protein (RAP).Protein science : a publication of the Protein Society · 2007Article
- NMR structural studies of domain 1 of receptor-associated protein.Journal of biomolecular NMR · 2004Article
- T cell lines specific for a synthetic Heymann nephritis peptide derived from the receptor-associated protein.Clinical and experimental immunology · 2000Article
- Localization of a single transglutaminase-reactive glutamine in the third domain of RAP, the alpha2-macroglobulin receptor-associated protein.Journal of protein chemistry · 1999Article
- Editing of multidimensional NMR spectra of partially deuterated proteins. Measurement of amide deuterium isotope effects on the chemical shifts of protein backbone nuclei.Journal of biomolecular NMR · 1998Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain.
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