Sandbox Reserved 958
From Proteopedia
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<Structure load='4NYF' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <Structure load='4NYF' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | '''Dimer of HIV-1 integrase catalytic core domain''' is the active form of the '''3'-Processing''' reaction that occurs in patients cells suffering from '''AIDS'''. The catalytic core domain is just one of three parts composing the HIV-1 integrase. This enzyme performs mainly two specific reactions : the '''3'-processing''' and the '''integration of the viral DNA''' into the host genome. ''In vivo'' we can find this protein in several forms such as monomer, dimers and tetramers<ref>http://www.retrovirology.com/content/5/1/114</ref>. | + | '''Dimer of HIV-1 integrase catalytic core domain''' is the active form of the '''3'-Processing''' reaction that occurs in patients cells suffering from '''AIDS'''. The catalytic core domain is just one of three parts composing the HIV-1 integrase. This enzyme performs mainly two specific reactions : the '''3'-processing''' and the '''integration of the viral DNA''' into the host genome. ''In vivo'' we can find this protein in several forms such as monomer, dimers and tetramers<ref name="Integrase and integration: biochemical activities of HIV-1 integrase">http://www.retrovirology.com/content/5/1/114</ref>. |
==Biological role== | ==Biological role== | ||
'''A'''cquired '''I'''mmune '''D'''efficiency '''S'''yndrome ('''AIDS''') is a human disease caused by the '''H'''uman '''I'''munnodeficiency '''V'''irus ('''HIV''') which is part of the retroviral virus family. This virus infects immune system's cells (Lymphocytes, Macrophages or Dendritic Cells,...) and provoke their destruction by highjacking the cellular machinery. | '''A'''cquired '''I'''mmune '''D'''efficiency '''S'''yndrome ('''AIDS''') is a human disease caused by the '''H'''uman '''I'''munnodeficiency '''V'''irus ('''HIV''') which is part of the retroviral virus family. This virus infects immune system's cells (Lymphocytes, Macrophages or Dendritic Cells,...) and provoke their destruction by highjacking the cellular machinery. | ||
Revision as of 15:01, 22 December 2014
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| This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975. |
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Dimer of HIV-1 integrase catalytic core domain is the active form of the 3'-Processing reaction that occurs in patients cells suffering from AIDS. The catalytic core domain is just one of three parts composing the HIV-1 integrase. This enzyme performs mainly two specific reactions : the 3'-processing and the integration of the viral DNA into the host genome. In vivo we can find this protein in several forms such as monomer, dimers and tetramers[1].
Contents |
Biological role
Acquired Immune Defficiency Syndrome (AIDS) is a human disease caused by the Human Imunnodeficiency Virus (HIV) which is part of the retroviral virus family. This virus infects immune system's cells (Lymphocytes, Macrophages or Dendritic Cells,...) and provoke their destruction by highjacking the cellular machinery.
In the first step the virus penetrates the cell through specific membrane receptors then the Retrotranscriptase transforms the viral RNA into a double strand DNA. Further, it will be integrated into the cellular DNA by association with the integrase and other viral and cellular proteins to form the Pre-Integration Complex (PIC). In the last step several viral proteins will be expressed and new virions will be formed by packaging viral and cellular proteins but also the viral RNA.
This process leads to an Imunnodeficiency that can indirectly undergo death by an opportunic infection.
Structure
DNA binding
Function
3'-Processing
Strand Transfer
Posttranslationnal Modifications
Inhibitors
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</StructureSection>
