scholarly journals HIV gp120; CC chemokine receptor 5 (CCR5; CD195); CXC chemokine receptor 4 (CXCR4; NPY3R)

2012 ◽  
Vol 5 (7) ◽  
pp. 181-181
2007 ◽  
Vol 56 (10) ◽  
pp. 1589-1595 ◽  
Author(s):  
Stefania Scala ◽  
Caterina Ieranò ◽  
Alessandro Ottaiano ◽  
Renato Franco ◽  
Anna La Mura ◽  
...  

2017 ◽  
Vol 25 (2) ◽  
pp. 646-657 ◽  
Author(s):  
Markus Baumann ◽  
Mohammad Musarraf Hussain ◽  
Nina Henne ◽  
Daniel Moya Garrote ◽  
Stefanie Karlshøj ◽  
...  

Hepatology ◽  
2003 ◽  
Vol 38 ◽  
pp. 736-736
Author(s):  
A FLOREANI ◽  
A TOMMASI ◽  
A BARAGIOTTA ◽  
V BALDO ◽  
G TOSITTI ◽  
...  

2012 ◽  
Vol 286 (1) ◽  
pp. 51-54 ◽  
Author(s):  
Figen Gurdol ◽  
Leman M. Yurdum ◽  
Ummühan Ozturk ◽  
Elif Isbilen ◽  
Bedia Cakmakoglu

2020 ◽  
Author(s):  
Polina Isaikina ◽  
Ching-Ju Tsai ◽  
Nikolaus Dietz ◽  
Filip Pamula ◽  
Anne Grahl ◽  
...  

AbstractThe human CC chemokine receptor 5 (CCR5) is a G protein-coupled receptor (GPCR) that plays a major role in inflammation and is involved in the pathology of cancer, HIV, and COVID-19. Despite its significance as a drug target, the activation mechanism of CCR5, i.e. how chemokine agonists transduce the activation signal through the receptor, is yet unknown. Here, we report the cryo-EM structure of wild-type CCR5 in an active conformation bound to the chemokine super-agonist [6P4]CCL5 and the heterotrimeric Gi protein. The structure provides the rationale for the sequence-activity relation of agonist and antagonist chemokines. The N-terminus of agonist chemokines pushes onto an aromatic connector that transmits activation to the canonical GPCR microswitch network. This activation mechanism differs significantly from other CC chemokine receptors that bind shorter chemokines in a shallow binding mode and have unique sequence signatures and a specialized activation mechanism.One-sentence summaryThe structure of CCR5 in complex with the chemokine agonist [6P4]CCL5 and the heterotrimeric Gi protein reveals its activation mechanism


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