VP24: Difference between revisions
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<StructureSection load='4d9o' size='340' side='right' caption='VP24 from the Reston Ebola Virus [[4d9o]]' scene=''> | <StructureSection load='4d9o' size='340' side='right' caption='VP24 from the Reston Ebola Virus [[4d9o]]' scene=''> | ||
== Introduction == | == Introduction == | ||
VP24 is a protein present in the Ebola and Marburg viruses, both of which are members of ''Filoviridae'' family. Presently there are five strains of Ebola: Sudan, Reston, Zaire, Bundibugyo, and Taï Forest, each with minor differences in VP24 sequences <ref name=' | VP24 is a protein present in the Ebola and Marburg viruses, both of which are members of ''Filoviridae'' family. Presently there are five strains of Ebola: Sudan, Reston, Zaire, Bundibugyo, and Taï Forest, each with minor differences in VP24 sequences <ref name='Marburg '>pmid 24574400</ref>. | ||
== Function == | == Function == | ||
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== Structural Characteristics == | == Structural Characteristics == | ||
The Ebola and Marburg VP24 proteins are 30% identical(1). They share a similar pyramidal shaped domain, as well as a few structures. Both viruses have two highly conserved pockets underneath the "pyramid's" base | The Ebola and Marburg VP24 proteins are 30% identical(1). They share a similar pyramidal shaped domain, as well as a few structures. Both viruses have two highly conserved pockets underneath the "pyramid's" base <ref name='Marburg '/>. Additionally, the N termini of Ebola (Zaire) and the Marburg virus are very similar in function. They are both used for oligomer and nucleocapsid formation <ref name='Marburg '/><ref>pmid 22371572</ref>. | ||
<scene name='60/602719/Chain_b/1'>Ebola Domain</scene> (Reston) | <scene name='60/602719/Chain_b/1'>Ebola Domain</scene> (Reston) | ||
There are a few structural characteristics only found in the Ebola viruses. At the top of the pyramidal domain, there are α helices present which are thought to interact with the α karyopherin <ref name=' | There are a few structural characteristics only found in the Ebola viruses. At the top of the pyramidal domain, there are α helices present which are thought to interact with the α karyopherin <ref name='Marburg '/>. An α helix formed by the N-terminus runs from the top of the "pyramid" to another nearby VP24, where it binds to one of the pockets located underneath the "pyramid" <ref name='Marburg '/>. | ||
<scene name='60/602719/Marburg_vp24_domain/1'>Marburg Domain</scene> | <scene name='60/602719/Marburg_vp24_domain/1'>Marburg Domain</scene> | ||
The Marburg domain has a beta shelf present that sticks out from the structure <ref name=' | The Marburg domain has a beta shelf present that sticks out from the structure <ref name='Marburg '/>. The Marburg VP24 doesn't use an alpha helix to bind to another VP24 like the Ebola VP24 <ref name='Marburg '/>. Instead, it uses a flexible strand that binds to a groove of a close-by VP24 <ref name='Marburg '/>. | ||
</StructureSection> | </StructureSection> | ||
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4. Edwards, R. M., Johnson, B., Mire, C.E., Xu, W., Shabman, R.S., Speller, L.N., Leung, D.W., Geisbert, T.W., Amarasinghe, G.K., Basler, C.F. The Marburg Virus VP24 Protein Interacts with Keap1 to Activate the Cytoprotective Antioxidant Response Pathway. Cell. 2014, Mar 27. 6 1017-1025 | 4. Edwards, R. M., Johnson, B., Mire, C.E., Xu, W., Shabman, R.S., Speller, L.N., Leung, D.W., Geisbert, T.W., Amarasinghe, G.K., Basler, C.F. The Marburg Virus VP24 Protein Interacts with Keap1 to Activate the Cytoprotective Antioxidant Response Pathway. Cell. 2014, Mar 27. 6 1017-1025 | ||
<references/> | <references/> | ||
