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Crystal structure of the receptor-binding domain of alpha 2-macroglobulin

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Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. / Jenner, L; Husted, L; Thirup, S; Sottrup-Jensen, L; Nyborg, J.

In: Structure, Vol. 6, No. 5, 1998, p. 595-604.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Jenner, L, Husted, L, Thirup, S, Sottrup-Jensen, L & Nyborg, J 1998, 'Crystal structure of the receptor-binding domain of alpha 2-macroglobulin', Structure, vol. 6, no. 5, pp. 595-604.

APA

Jenner, L., Husted, L., Thirup, S., Sottrup-Jensen, L., & Nyborg, J. (1998). Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. Structure, 6(5), 595-604.

CBE

MLA

Jenner, L et al. "Crystal structure of the receptor-binding domain of alpha 2-macroglobulin". Structure. 1998, 6(5). 595-604.

Vancouver

Author

Jenner, L ; Husted, L ; Thirup, S ; Sottrup-Jensen, L ; Nyborg, J. / Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. In: Structure. 1998 ; Vol. 6, No. 5. pp. 595-604.

Bibtex

@article{0526d150f9c011dd8f9a000ea68e967b,
title = "Crystal structure of the receptor-binding domain of alpha 2-macroglobulin",
abstract = "BACKGROUND: The large plasma proteinase inhibitors of the alpha 2-macroglobulin superfamily inhibit proteinases by capturing them within a central cavity of the inhibitor molecule. After reaction with the proteinase, the alpha-macroglobulin-proteinase complex binds to the alpha-macroglobulin receptor, present in the liver and other tissues, and becomes endocytosed and rapidly removed from the circulation. The complex binds to the receptor via recognition sites located on a separate domain of approximately 138 residues positioned at the C terminus of the alpha-macroglobulin subunit. RESULTS: The crystal structure of the receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been determined at a resolution of 1.9 A. The domain primarily comprises a nine-strand beta structure with a jelly-roll topology, but also contains two small alpha helices. CONCLUSIONS: The surface patch responsible for receptor recognition is thought to involve residues located on one of the two alpha helices of the bRBD as well as residues in two of the beta strands. Located on this alpha helix are two lysine residues that are important for receptor binding. The structure of bRBD is very similar to the approximately 100-residue C-terminal domain of factor XIII, a transglutaminase from the blood coagulation system.",
keywords = "Amino Acid Sequence, Animals, Binding Sites, Cattle, Crystallography, X-Ray, Factor XIII, LDL-Receptor Related Protein 1, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Folding, Protein Structure, Secondary, Receptors, Immunologic, Receptors, LDL, Sequence Homology, Amino Acid, alpha-Macroglobulins",
author = "L Jenner and L Husted and S Thirup and L Sottrup-Jensen and J Nyborg",
year = "1998",
language = "English",
volume = "6",
pages = "595--604",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - Crystal structure of the receptor-binding domain of alpha 2-macroglobulin

AU - Jenner, L

AU - Husted, L

AU - Thirup, S

AU - Sottrup-Jensen, L

AU - Nyborg, J

PY - 1998

Y1 - 1998

N2 - BACKGROUND: The large plasma proteinase inhibitors of the alpha 2-macroglobulin superfamily inhibit proteinases by capturing them within a central cavity of the inhibitor molecule. After reaction with the proteinase, the alpha-macroglobulin-proteinase complex binds to the alpha-macroglobulin receptor, present in the liver and other tissues, and becomes endocytosed and rapidly removed from the circulation. The complex binds to the receptor via recognition sites located on a separate domain of approximately 138 residues positioned at the C terminus of the alpha-macroglobulin subunit. RESULTS: The crystal structure of the receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been determined at a resolution of 1.9 A. The domain primarily comprises a nine-strand beta structure with a jelly-roll topology, but also contains two small alpha helices. CONCLUSIONS: The surface patch responsible for receptor recognition is thought to involve residues located on one of the two alpha helices of the bRBD as well as residues in two of the beta strands. Located on this alpha helix are two lysine residues that are important for receptor binding. The structure of bRBD is very similar to the approximately 100-residue C-terminal domain of factor XIII, a transglutaminase from the blood coagulation system.

AB - BACKGROUND: The large plasma proteinase inhibitors of the alpha 2-macroglobulin superfamily inhibit proteinases by capturing them within a central cavity of the inhibitor molecule. After reaction with the proteinase, the alpha-macroglobulin-proteinase complex binds to the alpha-macroglobulin receptor, present in the liver and other tissues, and becomes endocytosed and rapidly removed from the circulation. The complex binds to the receptor via recognition sites located on a separate domain of approximately 138 residues positioned at the C terminus of the alpha-macroglobulin subunit. RESULTS: The crystal structure of the receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been determined at a resolution of 1.9 A. The domain primarily comprises a nine-strand beta structure with a jelly-roll topology, but also contains two small alpha helices. CONCLUSIONS: The surface patch responsible for receptor recognition is thought to involve residues located on one of the two alpha helices of the bRBD as well as residues in two of the beta strands. Located on this alpha helix are two lysine residues that are important for receptor binding. The structure of bRBD is very similar to the approximately 100-residue C-terminal domain of factor XIII, a transglutaminase from the blood coagulation system.

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Cattle

KW - Crystallography, X-Ray

KW - Factor XIII

KW - LDL-Receptor Related Protein 1

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Protein Folding

KW - Protein Structure, Secondary

KW - Receptors, Immunologic

KW - Receptors, LDL

KW - Sequence Homology, Amino Acid

KW - alpha-Macroglobulins

M3 - Journal article

C2 - 9634697

VL - 6

SP - 595

EP - 604

JO - Structure

JF - Structure

SN - 0969-2126

IS - 5

ER -