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	<ref name="Bergoug">PMID:33121128</ref>		<ref name="Bergoug">PMID:33121128</ref>
	== Structure ==		== Structure ==
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	=== Conformation: Open ===		=== Conformation: Open ===

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Revision as of 19:40, 22 March 2022

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 Conformation: Open Conformation: Closed 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

• Hannah Luchinski