The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle
2007
Structure of the murine DLC2 SAM domain
publication
Evidence: moderate
Author Information
Author(s): Kwan Jamie J, Donaldson Logan W
Primary Institution: York University
Hypothesis
The study aims to understand the structure and function of the murine DLC2 SAM domain.
Conclusion
The DLC2-SAM domain adopts a structure that is more similar to a four-helix bundle than a canonical SAM domain, which may allow it to interact with new ligands.
Supporting Evidence
- The DLC2-SAM domain structure reveals an atypical four-helix composition.
- Helix 3 of the canonical SAM domain is replaced by shorter, extended secondary structure.
- The structure may allow DLC2 to interact with a novel set of ligands.
Takeaway
The DLC2 SAM domain has a unique shape that helps it interact with other molecules, which might be important for its role in preventing cancer.
Methodology
The structure was determined using nuclear magnetic resonance (NMR) spectroscopy.
Limitations
The study did not perform a detailed comparison with the human DLC2-SAM domain due to unavailability of coordinates.
Digital Object Identifier (DOI)
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