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Structure of the kinase domain of Gilgamesh from Drosophila melanogaster
Author(s) -
Han Ni,
Chen CuiCui,
Shi Zhubing,
Cheng Dianlin
Publication year - 2014
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/s2053230x14004774
Subject(s) - drosophila melanogaster , protein kinase domain , kinase , domain (mathematical analysis) , wnt signaling pathway , biology , chemistry , microbiology and biotechnology , stereochemistry , biochemistry , signal transduction , gene , mathematical analysis , mathematics , mutant
The CK1 family kinases regulate multiple cellular aspects and play important roles in Wnt/Wingless and Hedgehog signalling. The kinase domain of Drosophila Gilgamesh isoform I (Gilgamesh‐I), a homologue of human CK1‐γ, was purified and crystallized. Crystals of methylated Gilgamesh‐I kinase domain with a D210A mutation diffracted to 2.85 Å resolution and belonged to space group P 4 3 2 1 2, with unit‐cell parameters a = b = 52.025, c = 291.727 Å. The structure of Gilgamesh‐I kinase domain, which was determined by molecular replacement, has conserved catalytic elements and an active conformation. Structural comparison indicates that an extended loop between the α1 helix and the β4 strand exists in the Gilgamesh‐I kinase domain. This extended loop may regulate the activity and function of Gilgamesh‐I.