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

Adherens junctions transmit mechanical force between cells. In these junctions, β -catenin binds to cadherins and to the N-terminal domain of α -catenin, which in turn binds to actin filaments via its C-terminal domain. The middle (M) domain of α -catenin plays an important role in responding to mechanical tension. The nematode Caenorhabditis elegans contains α - and β -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 α -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 P3121, 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 P212121, 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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: α -catenin HMP-1 adherens junction Caenorhabditis elegans research communications Source Type: research

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