Gp41: Difference between revisions

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<StructureSection load='1aik' size='340' side='right' caption='Core structure of acetylated gp41 from the HIV envelope glycoprotein, [[1aik]].' scene=''>
<StructureSection load='1aik' size='340' side='right' caption='Core structure of acetylated gp41 from the HIV envelope glycoprotein, [[1aik]].' scene=''>
== Function ==
== Function ==
'''Gp41''' is a subunit of the envelope protein of retrovirus<ref>PMID:9630213</ref>.  Gp41 is a transmembrane protein and contains several sites which are involved in the infection of the host cells. Gp160 is the cleavable precursor of Gp41 and Gp120.  For more details see [[Hiv env proteins]].
'''Gp41''' is a subunit of the envelope protein of retrovirus<ref>PMID:9630213</ref>.  Gp41 is a transmembrane protein and contains several sites which are involved in the infection of the host cells. Gp160 is the cleavable precursor of Gp41 and Gp120.  For more details see [[Hiv env proteins|HIV-1 viral envelope proteins]].


== Relevance ==
== Relevance ==
Fusion inhibitory drugs which bind to Gp41 prevent the attachment of the HIV-1 virus to the cell<ref>PMID:15180542</ref>.
Fusion inhibitory drugs which bind to Gp41 prevent the attachment of the HIV-1 virus to the cell<ref>PMID:15180542</ref>.
</StructureSection>
 
== 3D Structures of Gp41 ==
== 3D Structures of Gp41 ==
[[Gp41 3D Structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Gp41 from HIV-1; Domains – core 509-661; N-peptide 541-590; transmembrane 670-709; tail 750-854
 
**[[2zfc]], [[3u91]] – Gp41 N-terminal residues 1-49 <br />
**[[3k9a]] – Gp41 residues 1-108 (mutant)<br />
**[[1aik]], [[1df4]], [[1df5]], [[1qr8]], [[1qr9]], [[1dlb]], [[1jpx]], [[1szt]], [[3vu5]], [[3vu6]] - Gp41 N-peptide domain <br />
**[[1env]], [[3cp1]], [[3cyo]], [[1f23]], [[1k33]], [[1k34]], [[1i5x]], [[1i5y]], [[2ot5]], [[5ka6]], [[5ka5]], [[4i2l]] – Gp41 N-peptide domain (mutant)<br />
**[[2z2t]], [[2zzo]], [[3aha]], [[3vie]], [[2r3c]], [[2r5b]], [[2r5d]], [[3l36]], [[3l37]], [[3vgy]], [[3vh7]], [[3vtp]], [[5h0n]]  – Gp41 N-peptide domain + fusion inhibitor peptide<br />
**[[6b3u]] – Gp41 transmembrane domain - NMR<br />
**[[5vwl]] – Gp41 tail domain - NMR<br />
**[[5v8l]], [[5v8m]], [[5uty]], [[5utf]], [[5um8]], [[5jsa]], [[5js9]], [[5i8h]], [[5d9q]], [[5cjx]], [[5c7k]], [[6ck9]], [[6chb]], [[6ch9]], [[6ch8]], [[6ch7]], [[5w6d]], [[4nrx]], [[5fyk]], [[5fyj]], [[4nco]] – Gp41 core + Gp120 + antibody<br />
**[[6cdi]] – Gp41 core + Gp120 + antibody – Cryo EM<br />
**[[5u1f]], [[5thr]] – Gp41 core + Gp120 + antibody + CD4<br />
**[[5hm1]] – Gp41 core + llama  antibody <br />
**[[3o3x]] – arGp41 - artificial<br />
**[[4dzu]] – arGp41 + 3-α<br />
**[[4dzv]] – arGp41 + 4-α/β<br />
 
*Gp41 from Simian Immunodeficiency Virus


**[[2siv]] – Gp41 core<br />
**[[2ezo]], [[2ezp]], [[2ezq]], [[2ezr]], [[2ezs]], [[1qce]] – Gp41 core - NMR<br />
**[[1qbz]], [[1jq0]] – Gp41 core (mutant)<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 17:57, 17 November 2019

Function

Gp41 is a subunit of the envelope protein of retrovirus[1]. Gp41 is a transmembrane protein and contains several sites which are involved in the infection of the host cells. Gp160 is the cleavable precursor of Gp41 and Gp120. For more details see HIV-1 viral envelope proteins.

Relevance

Fusion inhibitory drugs which bind to Gp41 prevent the attachment of the HIV-1 virus to the cell[2].

3D Structures of Gp41

Gp41 3D Structures


Core structure of acetylated gp41 from the HIV envelope glycoprotein, 1aik.

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Chan DC, Kim PS. HIV entry and its inhibition. Cell. 1998 May 29;93(5):681-4. PMID:9630213
  2. Root MJ, Steger HK. HIV-1 gp41 as a target for viral entry inhibition. Curr Pharm Des. 2004;10(15):1805-25. PMID:15180542

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky