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G-protein coupled receptors (GPCRs) are the “inbox” of environmental messages in mammalian cells. Due to their central function in signaling pathways, mutations leading to irregular GPCR capabilities trigger all kinds of illnesses. Subsequently, GPCRs are essentially the most intensively studied drug targets.

After activation, GPCRs should be deactivated by enzymes known as GPCR kinases and a household of proteins known as arrestins. Intriguingly, whereas there are lots of of GPCR subtypes, mammals have solely 4 arrestins. One area the place arrestin subtypes differ is the protein’s “finger loop” within the middle of the receptor-binding floor.

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Now in a examine printed within the journal PLOS ONE, Vsevolod Gurevich, Ph.D., and colleagues present {that a} glycine residue firstly of the finger loop is important for the arrestin-GPCR interplay.

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Their work demonstrates that the flexibility of arrestin to “mildew” itself to suit into the GPCR advanced is extra necessary for receptor binding than the precise protein sequence in different arrestin components.

How proteins discover each other

Extra data:
Chen Zheng et al. Important function of the finger loop in arrestin binding to the receptors, PLOS ONE (2019). DOI: 10.1371/journal.pone.0213792

Supplied by
Vanderbilt College

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The arrestin-GPCR connection (2019, April 15)
retrieved 15 April 2019

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