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Structure of the kinase domain of Gilgamesh from Drosophila melanogaster.

ABSTRACT: 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-?, 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 P43212, 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 ?1 helix and the ?4 strand exists in the Gilgamesh-I kinase domain. This extended loop may regulate the activity and function of Gilgamesh-I.

SUBMITTER: Han N

PROVIDER: S-EPMC3976058 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Structure of the kinase domain of Gilgamesh from Drosophila melanogaster.

Han Ni N Chen CuiCui C Shi Zhubing Z Cheng Dianlin D

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4

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 P43212, with unit-cell parameters a = b = 52.025, c = 291.727 Å. The structure of Gilgamesh-I kinase domain, which was ...[more]

PMID: 24699734

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