Neurofibromin

spinqualitylabelsall models Neurofibromin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structure Important Structural Features Arginine Finger The catalytic glutamine is too far away in the GDP bound form to perform any function. The arginine finger stabilizes glutamine which assists the cleaving mechanism. RAS Complex NF interacts with Ras to form a complex. R68 assists N61 in catalysis. Mechanism of Ras Coupled with Neurofibromin The RasGAP interactions that occur when neurofibromin's GAP domain and Ras are bound have two critical catalytic components. The first is the arginine finger Figure X Downstream Effects Figure X; By cybertory - This file was derived from: Signal transduction v1.png, CC BY-SA 3.0, https://commons.wikimedia.org/w/index.php?curid=12081090 Disease Relevance Mutations to the neurofibromin protein are implicated in the progression of Neurofibromatosis type 1 (NF1). This condition drives several forms of human cancers by inactivating the Ras suppression effects of NF, allowing Ras to behave as an oncogene. Neurofibromatosis type 1 is an autosomal dominant disorder that affects 1 in 3,000 people, and the NF gene itself has the highest mutation rate of any known human gene, adding to its prevalence. NF1 primarily causes tumors in the central and peripheral nervous systems, but often has a multisystem expression including tumors in the dermatologic, cardiovascular, gastrointestinal, and orthopedic systems. The wide range of presentations is consistent with the multiplicity of mutations observed in the causative protein. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Proteopedia Page Contributors and Editors (what is this?)

Jordyn K. Lenard, Ryan D. Adkins, OCA, Michal Harel, Jaime Prilusky