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Neurofibromin

spinqualitylabelsall models Closed conformation of Neurofibromin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image --- [1] Figure_1 Contents 1 Introduction 2 Structure 2.1 Conformation: Open 2.2 Conformation: Closed 2.3 Domains 2.4 Key Players 3 Function 3.1 Ras Control 3.2 Mutated 4 Diseases Introduction [1] Structure Neurofibromin is a with two identical chains (depicted as lime and cyan). Conformation: Open Conformation: Closed In the overall closed and inactive conformation of the neurofibromin protein, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive. The closed conformation is much more tightly compacted and there is no room for association with the Ras protein. Domains Key Players Function Ras Control Mutated Diseases [2]

References

1. ↑ Bergoug M, Doudeau M, Godin F, Mosrin C, Vallee B, Benedetti H. Neurofibromin Structure, Functions and Regulation. Cells. 2020 Oct 27;9(11). pii: cells9112365. doi: 10.3390/cells9112365. PMID:33121128 doi:http://dx.doi.org/10.3390/cells9112365
2. ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677

Student Contributors

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