Crystal Structure of the SIKE1 Coiled-coil Domain in the Hippo STRIPAK Complex

A crystallographic study from the Center for Excellence in Molecular Cell Science reveals atomic-resolution interfaces within a Hippo kinase-containing STRIPAK complex. The data defines the structure of the second coiled-coil domain of SIKE1 and its interactions with STRN3 and SLMAP. This work provides a structural framework for understanding the dynamic, phosphorylation-dependent assembly of the STRIPAK complex and its regulation of Hippo signaling.

Use Cases

• Predicting protein-protein interaction interfaces based on the atomic-resolution crystal structures of STRN3-SIKE1 and SIKE1-SLMAP.
• Modeling the dynamic assembly of supramolecular complexes based on the described 'two-arm' mechanism and phosphorylation-dependent loading.
• Validating computational docking simulations for coiled-coil domain interactions using the reported crystallographic data.

Strengths

• Atomic-resolution structural data from crystallographic studies provides high-detail molecular interfaces.
• The description details a specific biological mechanism ('two-arm' assembly) and its regulatory context (phosphorylation, cell density).

Limitations

• The specific data format, column definitions, and row count are unknown, limiting technical assessment.
• The dataset's availability, file formats, and sample data are not described in the input metadata.

Provenance

Source

Center for Excellence in Molecular Cell Science

Collection Method

Crystallographic studies reported in a research paper.