Recombinant Xenopus laevis Protein slowmo homolog 1 (slmo1) is a protein of interest in molecular biology, particularly in studies involving protein-protein interactions and cellular processes. While specific details about this protein might be limited, related proteins like SLMO1 in other organisms have been studied extensively. For instance, SLMO1 in humans is known to interact with TRIAP1, a protein involved in mitochondrial phospholipid metabolism . This article will delve into the available information on slmo1 and related proteins, focusing on their structure, function, and interactions.
SLMO1 interacts with TRIAP1 via a hydrophobic stripe, which is crucial for their complex formation. Mutagenesis studies have identified key residues at the interface, such as V36 and L49 in SLMO1, which are essential for maintaining the interaction . The TRIAP1-SLMO1 complex plays a role in supplying phosphatidic acid to the inner mitochondrial membrane, highlighting its importance in mitochondrial phospholipid metabolism.
| Key Residues | Protein | Role in Interaction |
|---|---|---|
| V36, L49 | SLMO1 | Essential for complex formation |
| F41 | TRIAP1 | Key interfacial contact |
Research on SLMO1 and related proteins has implications for understanding mitochondrial function and phospholipid metabolism. The conservation of structural features across species suggests a conserved mechanism of action. Further studies on recombinant Xenopus laevis Protein slowmo homolog 1 could provide insights into its specific role in cellular processes and potential applications in biotechnology or biomedical research.
KEGG: xla:444585
UniGene: Xl.29441