Authors:

Ayana Price

Date Created:

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About Paper:

Research has shown that protein SOCS1 dimer has higher affinity to JAK2 than SOCS1 monomer. SOCS1 plays an integral role in the JAK-STAT pathway. The JAK-STAT signaling pathway is involved in the processes of immunity, cell division and cell death. SOCS1 is inhibits JAK from binding which will down-regulate the signaling events. Bioinformatic tools and AI were used to analyze protein- protein interactions. Using Hipergator, AlphaFold generated 3D models of JAK2 and SOCS1 multimers. AlphaFold's precision aided in creating accurate models, enabling us to analyze bonding angles, rotations, and protein folding. Through these comparisons, we gain insights into the reasons behind the superior binding of the SOCS1-KIR dimer, providing a visual understanding of their interactions. Stability checks on each structure ensured they were accurate. The Ramachandran plot of SOCS1 monomer revealed many amino acids in disallowed regions. This suggests that there may be structure distortions in the protein's conformation due to strained conformations or misfolding. Structural complications of SOCS1 will lead to inflammation and autoimmune disorders. In forthcoming studies, we will investigate the evolutionary dynamics across diverse species to analyze the conformational changes of JAK2, JAK1, JAK3, SOCS1, and TYK2. Thus, revealing which mutations are driving this function. 499

Source:

University of Florida / 2024

Topics:

No topics listed

Co-authors:

Ayana Price