Purification, crystallization and initial crystallographic analysis of the ?-catenin homologue HMP-1 from Caenorhabditis elegans.

ABSTRACT: Adherens junctions transmit mechanical force between cells. In these junctions, ?-catenin binds to cadherins and to the N-terminal domain of ?-catenin, which in turn binds to actin filaments via its C-terminal domain. The middle (M) domain of ?-catenin plays an important role in responding to mechanical tension. The nematode Caenorhabditis elegans contains ?- and ?-catenin homologues called HMP-1 and HMP-2, respectively, but HMP-1 behaves differently from its mammalian homologue. Thus, structural and biochemical studies of HMP-1 have been initiated to understand the mechanism of HMP-1 and the evolution of ?-catenin. The N-terminal domain of HMP-1 in complex with the minimal HMP-1-binding region of HMP-2 was purified and crystallized. These crystals diffracted to 1.6 Å resolution and belonged to space group P3(1)21, with unit-cell parameters a = b = 57.1, c = 155.4 Å. The M domain of HMP-1 was also purified and crystallized. The M-domain crystals diffracted to 2.4 Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 72.8, b = 81.5, c = 151.4 Å. Diffraction data were collected and processed from each crystal, and the structures were solved by molecular replacement.

SUBMITTER: Kang H 

PROVIDER: S-EPMC4774883 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature