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Structure and binding properties of a cameloid nanobody raised against KDM5B
Author(s) -
Wiuf Anders,
Kristensen Line Hyltoft,
Kristensen Ole,
Dorosz Jerzy,
Jensen Jonas,
Gajhede Michael
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1501537x
Subject(s) - demethylase , crystallization , monomer , crystallography , molecule , chemistry , crystal structure , resolution (logic) , histone , biophysics , stereochemistry , biochemistry , biology , dna , polymer , organic chemistry , artificial intelligence , computer science
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 P 4 3 22 with six molecules in the asymmetric unit. The six molecules in the asymmetric unit pack as an entity with approximate D 3 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.