Structure and binding properties of a cameloid nanobody raised against KDM5B

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Standard

Structure and binding properties of a cameloid nanobody raised against KDM5B. / Wiuf, Anders; Kristensen, Line Hyltoft; Kristensen, Ole; Dorosz, Jerzy; Jensen, Jonas; Gajhede, Michael.

In: Acta crystallographica. Section F, Structural biology communications, Vol. 71, No. Pt 10, 23.09.2015, p. 1235-1241.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wiuf, A, Kristensen, LH, Kristensen, O, Dorosz, J, Jensen, J & Gajhede, M 2015, 'Structure and binding properties of a cameloid nanobody raised against KDM5B', Acta crystallographica. Section F, Structural biology communications, vol. 71, no. Pt 10, pp. 1235-1241. https://doi.org/10.1107/S2053230X1501537X

APA

Wiuf, A., Kristensen, L. H., Kristensen, O., Dorosz, J., Jensen, J., & Gajhede, M. (2015). Structure and binding properties of a cameloid nanobody raised against KDM5B. Acta crystallographica. Section F, Structural biology communications, 71(Pt 10), 1235-1241. https://doi.org/10.1107/S2053230X1501537X

Vancouver

Wiuf A, Kristensen LH, Kristensen O, Dorosz J, Jensen J, Gajhede M. Structure and binding properties of a cameloid nanobody raised against KDM5B. Acta crystallographica. Section F, Structural biology communications. 2015 Sep 23;71(Pt 10):1235-1241. https://doi.org/10.1107/S2053230X1501537X

Author

Wiuf, Anders ; Kristensen, Line Hyltoft ; Kristensen, Ole ; Dorosz, Jerzy ; Jensen, Jonas ; Gajhede, Michael. / Structure and binding properties of a cameloid nanobody raised against KDM5B. In: Acta crystallographica. Section F, Structural biology communications. 2015 ; Vol. 71, No. Pt 10. pp. 1235-1241.

Bibtex

@article{db1fd5e858104bd682818e931e3baeb1,
title = "Structure and binding properties of a cameloid nanobody raised against KDM5B",
abstract = "The histone demethylase KDM5B is considered to be a promising target for anticancer therapy. Single-chain antibodies from llama (nanobodies) have been raised to aid in crystallization and structure determination of this enzyme. The antigen-binding properties of 15 of these nanobodies have been characterized. The crystal structure of one of these (NB17) has been determined to a resolution of 1.85 {\AA}. NB17 crystallizes in space group P4322 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximate D3 symmetry with interactions mediated by the CDR loops, which could act as a crystallization nucleus. NB17 does not bind to monomeric KDM5B residues 1-820, but is found to bind to aggregates formed after incubation at 310 K.",
author = "Anders Wiuf and Kristensen, {Line Hyltoft} and Ole Kristensen and Jerzy Dorosz and Jonas Jensen and Michael Gajhede",
year = "2015",
month = sep,
day = "23",
doi = "10.1107/S2053230X1501537X",
language = "English",
volume = "71",
pages = "1235--1241",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 10",

}

RIS

TY - JOUR

T1 - Structure and binding properties of a cameloid nanobody raised against KDM5B

AU - Wiuf, Anders

AU - Kristensen, Line Hyltoft

AU - Kristensen, Ole

AU - Dorosz, Jerzy

AU - Jensen, Jonas

AU - Gajhede, Michael

PY - 2015/9/23

Y1 - 2015/9/23

N2 - The histone demethylase KDM5B is considered to be a promising target for anticancer therapy. Single-chain antibodies from llama (nanobodies) have been raised to aid in crystallization and structure determination of this enzyme. The antigen-binding properties of 15 of these nanobodies have been characterized. The crystal structure of one of these (NB17) has been determined to a resolution of 1.85 Å. NB17 crystallizes in space group P4322 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximate D3 symmetry with interactions mediated by the CDR loops, which could act as a crystallization nucleus. NB17 does not bind to monomeric KDM5B residues 1-820, but is found to bind to aggregates formed after incubation at 310 K.

AB - The histone demethylase KDM5B is considered to be a promising target for anticancer therapy. Single-chain antibodies from llama (nanobodies) have been raised to aid in crystallization and structure determination of this enzyme. The antigen-binding properties of 15 of these nanobodies have been characterized. The crystal structure of one of these (NB17) has been determined to a resolution of 1.85 Å. NB17 crystallizes in space group P4322 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximate D3 symmetry with interactions mediated by the CDR loops, which could act as a crystallization nucleus. NB17 does not bind to monomeric KDM5B residues 1-820, but is found to bind to aggregates formed after incubation at 310 K.

U2 - 10.1107/S2053230X1501537X

DO - 10.1107/S2053230X1501537X

M3 - Journal article

C2 - 26457512

VL - 71

SP - 1235

EP - 1241

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 10

ER -

ID: 145930551