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The loop region around amino acid residue 50, the N-terminal part of the alpha-helix, and the C-terminus of human retinol-binding protein are not located in or close to the transthyretin binding site
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. (osteo)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
1995 (English)In: Biochemistry and Molecular Biology International, ISSN 1039-9712, Vol. 37, no 6, 1147-1151 p.Article in journal (Refereed) Published
Abstract [en]

Although the three-dimensional structures of both human retinol-binding protein (RBP) and transthyretin (TTR) are known, the binding sites have not been defined. In this study we have epitope-mapped a rabbit antiserum against human RBP using synthetic peptides corresponding to all potentially antigenic sites. Immunoreactivity was seen with peptides corresponding to amino acid residues 46-54, 137-146, 143-153, and 172-182 of RBP. Since previous studies have demonstrated that these antibodies bind equally well to free RBP and to the RBP-TTR complex, we conclude that neither the loop region around amino acid residue 50, the N-terminal part of the alpha-helix, nor the C-terminus of RBP is located in or close to the TTR binding site. Our results support the hypothesis that one of the entrance loops is involved in the TTR binding.

Place, publisher, year, edition, pages
1995. Vol. 37, no 6, 1147-1151 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-55164PubMedID: 8747545OAI: oai:DiVA.org:uu-55164DiVA: diva2:83072
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-04Bibliographically approved

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