Purification, crystallization and preliminary X-ray diffraction studies of the ?-catenin homolog HMP-2 from Caenorhabditis elegans.

ABSTRACT: ?-Catenin is a multifunctional protein involved in both cell adhesion and Wnt signaling in metazoans. The nematode Caenorhabditis elegans is unusual in that it expresses four ?-catenin paralogs with separate functions. C. elegans HMP-2 participates in cell adhesion but not in Wnt signaling, so structural and biochemical studies of this protein will help in understanding its unusual specialization and the evolution of ?-catenin. HMP-2 was expressed, purified and crystallized in two different salt conditions. Crystals grown from a sodium formate condition diffracted to a resolution of 2?Å and belonged to space group C2, with unit-cell parameters a = 165.2, b = 39.0, c = 101.1?Å, ? = 116.7°. Crystals obtained from a lithium sulfate condition diffracted to 3?Å resolution and belonged to space group P43, with unit-cell parameters a = b = 85.3, c = 138.7?Å. Diffraction data were collected and processed from both crystal forms and the structure was solved by molecular replacement. Model refinement is in progress.

SUBMITTER: Choi HJ 

PROVIDER: S-EPMC4356301 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature