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• W2049643539 abstract "The α2macroglobulin-receptor-associated protein (RAP) binds to the α2macroglobulin receptor/low-density lipoprotein receptor-related protein (α2MR/LRP), a multi-functional cell surface receptor known to bind and internalize several macromolecular ligands. RAP has been shown to inhibit binding of all known α2MR/LRP ligands. Mutational studies have implicated distinct parts of RAP as specifically involved in inhibition of binding of a multitude of ligands. In the present paper we provide experimental evidence allowing assignment of elements of triplicate internal sequence similarity in RAP, noted previously [Warshawsky, I., Bu, G. & Schwartz, A. L. (1995) Sites within the 39-kDa protein important for regulating ligand binding to the low-density lipoprotein receptor-related protein, Biochemistry 34, 3404–3415], to three structural domains, 1, 2 and 3, comprising residues 18–112, 113–218 and 219–323 of RAP, respectively. Structural analysis by 1H-NMR spectroscopy shows that domains 1 and 2 as separate domains have similar secondary structures, consisting almost exclusively of α-helices, whereas domain 3 as a separate domain appears only to be marginally stable. Ligand competition titration of recombinant RAP domains 1, 2 and 3 and double domains 1+2 and 2+3 against 125I-RAP and 125I-α2M* (methylamine-activated α2M) for binding to α2MR*LRP demonstrated (a) that functional integrity in single domains is largely preserved, and (b) that important determinants for the inhibition of test ligands reside in the C-terminal regions of domains 1 and 3." @default.
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• W2049643539 date "1997-03-01" @default.
• W2049643539 modified "2023-09-25" @default.
• W2049643539 title "Dissection of the Domain Architecture of the alpha2macroglobulin-Receptor-Associated Protein" @default.
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• W2049643539 doi "https://doi.org/10.1111/j.1432-1033.1997.00544.x" @default.
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