Ras GTPase-activating protein-binding protein

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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'''Ras GTPase-activating protein-binding protein''' (G3BP) is a stress-granule protein that nucletes stress-granule assembly. Stress-granules are sites of mRNA storage that form by stress conditions like viral infection <ref>PMID:31500725</ref>
 
== Function ==
== Function ==
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'''Ras GTPase-activating protein-binding protein''' (G3BP) is a stress-granule protein that nucletes stress-granule assembly. Stress-granules are sites of mRNA storage that form by stress conditions like viral infection <ref>PMID:31500725</ref>.
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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G3BP1 contains an N-terminal nuclear transfer factor 2 (NTF2-like) domain, RNA recognition motif domain and Arg-Gly-rich region<ref>PMID:33349931</ref>.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Revision as of 07:34, 21 April 2024

Caption for this structure

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References

  1. Pandey K, Zhong S, Diel DG, Hou Y, Wang Q, Nelson E, Wang X. GTPase-activating protein-binding protein 1 (G3BP1) plays an antiviral role against porcine epidemic diarrhea virus. Vet Microbiol. 2019 Sep;236:108392. PMID:31500725 doi:10.1016/j.vetmic.2019.108392
  2. Sidibé H, Dubinski A, Vande Velde C. The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease. J Neurochem. 2021 May;157(4):944-962. PMID:33349931 doi:10.1111/jnc.15280

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Michal Harel, Alexander Berchansky

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