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Room temperature structure of human IgG4-Fc from crystals analysed in situ

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Room temperature structure of human IgG4-Fc from crystals analysed in situ. / Davies, Anna M.; Rispens, Theo; Ooijevaar-de Heer, Pleuni; Aalberse, Rob C.; Sutton, Brian J.

In: Molecular Immunology, Vol. 81, 01.2017, p. 85-91.

Research output: Contribution to journalArticle

Harvard

Davies, AM, Rispens, T, Ooijevaar-de Heer, P, Aalberse, RC & Sutton, BJ 2017, 'Room temperature structure of human IgG4-Fc from crystals analysed in situ', Molecular Immunology, vol. 81, pp. 85-91. https://doi.org/10.1016/j.molimm.2016.11.021

APA

Davies, A. M., Rispens, T., Ooijevaar-de Heer, P., Aalberse, R. C., & Sutton, B. J. (2017). Room temperature structure of human IgG4-Fc from crystals analysed in situ. Molecular Immunology, 81, 85-91. https://doi.org/10.1016/j.molimm.2016.11.021

Vancouver

Davies AM, Rispens T, Ooijevaar-de Heer P, Aalberse RC, Sutton BJ. Room temperature structure of human IgG4-Fc from crystals analysed in situ. Molecular Immunology. 2017 Jan;81:85-91. https://doi.org/10.1016/j.molimm.2016.11.021

Author

Davies, Anna M. ; Rispens, Theo ; Ooijevaar-de Heer, Pleuni ; Aalberse, Rob C. ; Sutton, Brian J. / Room temperature structure of human IgG4-Fc from crystals analysed in situ. In: Molecular Immunology. 2017 ; Vol. 81. pp. 85-91.

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@article{949b7345b6df4351a2e90a0cb860b185,
title = "Room temperature structure of human IgG4-Fc from crystals analysed in situ",
abstract = "The Fc region of IgG antibodies (Cγ2 and Cγ3 domains) is responsible for effector functions such as antibody-dependent cell-mediated cytotoxicity and phagocytosis, through engagement with Fcγ receptors, although the ability to elicit these functions differs between the four human IgG subclasses. A key determinant of Fcγ receptor interactions is the FG loop in the Cγ2 domain. High resolution cryogenic IgG4-Fc crystal structures have revealed a unique conformation for this loop, which could contribute to the particular biological properties of this subclass. To further explore the conformation of the IgG4 Cγ2 FG loop at near-physiological temperature, we solved a 2.7 {\AA} resolution room temperature structure of recombinant human IgG4-Fc from crystals analysed in situ. The Cγ2 FG loop in one chain differs from the cryogenic structure, and adopts the conserved conformation found in IgG1-Fc; however, this conformation participates in extensive crystal packing interactions. On the other hand, at room temperature, and free from any crystal packing interactions, the Cγ2 FG loop in the other chain adopts the conformation previously observed in the cryogenic IgG4-Fc structures, despite both conformations being accessible. The room temperature human IgG4-Fc structure thus provides a more complete and physiologically relevant description of the conformation of this functionally critical Cγ2 FG loop.",
keywords = "Antibody, IgG4, Immunoglobulin, X-ray crystallography",
author = "Davies, {Anna M.} and Theo Rispens and {Ooijevaar-de Heer}, Pleuni and Aalberse, {Rob C.} and Sutton, {Brian J.}",
year = "2017",
month = "1",
doi = "10.1016/j.molimm.2016.11.021",
language = "English",
volume = "81",
pages = "85--91",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Elsevier Limited",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - Room temperature structure of human IgG4-Fc from crystals analysed in situ

AU - Davies, Anna M.

AU - Rispens, Theo

AU - Ooijevaar-de Heer, Pleuni

AU - Aalberse, Rob C.

AU - Sutton, Brian J.

PY - 2017/1

Y1 - 2017/1

N2 - The Fc region of IgG antibodies (Cγ2 and Cγ3 domains) is responsible for effector functions such as antibody-dependent cell-mediated cytotoxicity and phagocytosis, through engagement with Fcγ receptors, although the ability to elicit these functions differs between the four human IgG subclasses. A key determinant of Fcγ receptor interactions is the FG loop in the Cγ2 domain. High resolution cryogenic IgG4-Fc crystal structures have revealed a unique conformation for this loop, which could contribute to the particular biological properties of this subclass. To further explore the conformation of the IgG4 Cγ2 FG loop at near-physiological temperature, we solved a 2.7 Å resolution room temperature structure of recombinant human IgG4-Fc from crystals analysed in situ. The Cγ2 FG loop in one chain differs from the cryogenic structure, and adopts the conserved conformation found in IgG1-Fc; however, this conformation participates in extensive crystal packing interactions. On the other hand, at room temperature, and free from any crystal packing interactions, the Cγ2 FG loop in the other chain adopts the conformation previously observed in the cryogenic IgG4-Fc structures, despite both conformations being accessible. The room temperature human IgG4-Fc structure thus provides a more complete and physiologically relevant description of the conformation of this functionally critical Cγ2 FG loop.

AB - The Fc region of IgG antibodies (Cγ2 and Cγ3 domains) is responsible for effector functions such as antibody-dependent cell-mediated cytotoxicity and phagocytosis, through engagement with Fcγ receptors, although the ability to elicit these functions differs between the four human IgG subclasses. A key determinant of Fcγ receptor interactions is the FG loop in the Cγ2 domain. High resolution cryogenic IgG4-Fc crystal structures have revealed a unique conformation for this loop, which could contribute to the particular biological properties of this subclass. To further explore the conformation of the IgG4 Cγ2 FG loop at near-physiological temperature, we solved a 2.7 Å resolution room temperature structure of recombinant human IgG4-Fc from crystals analysed in situ. The Cγ2 FG loop in one chain differs from the cryogenic structure, and adopts the conserved conformation found in IgG1-Fc; however, this conformation participates in extensive crystal packing interactions. On the other hand, at room temperature, and free from any crystal packing interactions, the Cγ2 FG loop in the other chain adopts the conformation previously observed in the cryogenic IgG4-Fc structures, despite both conformations being accessible. The room temperature human IgG4-Fc structure thus provides a more complete and physiologically relevant description of the conformation of this functionally critical Cγ2 FG loop.

KW - Antibody

KW - IgG4

KW - Immunoglobulin

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=85010190082&partnerID=8YFLogxK

U2 - 10.1016/j.molimm.2016.11.021

DO - 10.1016/j.molimm.2016.11.021

M3 - Article

AN - SCOPUS:85010190082

VL - 81

SP - 85

EP - 91

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

ER -

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