Vpr protein: Difference between revisions

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== Relevance ==

~~According to~~ 2017, the currently approved anti-HIV drugs target the Pol and Env encoded proteins. These drugs are effective in reducing viral replication. Thus, because of spontaneous mutations that occur during viral replication, drug resistance is evolve<ref>PMID:28681118</ref>. Understanding of Vpr structure and molecular mechanism may facilitate the design of HIV-1 antiviral therapy by its inhibition. Deletion of both ''vpr'' and ''vpx'' genes in SIV, which their protein products in SIV combine Vpr function in HIV-1, eliminate virus replication<ref name='Emerman1996'/>. The multiple significant functions that Vpr fills in HIV-1 replication makes it an attractive candidate for antiviral therapy<ref name='Gonzalez2017'/>.

As of now (October 2017), the currently approved anti-HIV drugs target the Pol and Env encoded proteins. These drugs are effective in reducing viral replication. Thus, because of spontaneous mutations that occur during viral replication, drug resistance is evolve<ref>PMID:28681118</ref>. Understanding of Vpr structure and molecular mechanism may facilitate the design of HIV-1 antiviral therapy by its inhibition. Deletion of both ''vpr'' and ''vpx'' genes in SIV, which their protein products in SIV combine Vpr function in HIV-1, eliminate virus replication<ref name='Emerman1996'/>. The multiple significant functions that Vpr fills in HIV-1 replication makes it an attractive candidate for antiviral therapy<ref name='Gonzalez2017'/>.

== Structural highlights<ref>PMID:12614620</ref> ==

Vpr protein: Difference between revisions

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@@ Line 14: / Line 14: @@
 == Relevance ==
-According to 2017, the currently approved anti-HIV drugs target the Pol and Env encoded proteins. These drugs are effective in reducing viral replication. Thus, because of spontaneous mutations that occur during viral replication, drug resistance is evolve<ref>PMID:28681118</ref>. Understanding of Vpr structure and molecular mechanism may facilitate the design of HIV-1 antiviral therapy by its inhibition. Deletion of both ''vpr'' and ''vpx'' genes in SIV, which their protein products in SIV combine Vpr function in HIV-1, eliminate virus replication<ref name='Emerman1996'/>. The multiple significant functions that Vpr fills in HIV-1 replication makes it an attractive candidate for antiviral therapy<ref name='Gonzalez2017'/>.
+As of now (October 2017), the currently approved anti-HIV drugs target the Pol and Env encoded proteins. These drugs are effective in reducing viral replication. Thus, because of spontaneous mutations that occur during viral replication, drug resistance is evolve<ref>PMID:28681118</ref>. Understanding of Vpr structure and molecular mechanism may facilitate the design of HIV-1 antiviral therapy by its inhibition. Deletion of both ''vpr'' and ''vpx'' genes in SIV, which their protein products in SIV combine Vpr function in HIV-1, eliminate virus replication<ref name='Emerman1996'/>. The multiple significant functions that Vpr fills in HIV-1 replication makes it an attractive candidate for antiviral therapy<ref name='Gonzalez2017'/>.
 == Structural highlights<ref>PMID:12614620</ref> ==