Sandbox Reserved 1722: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Paola Ariza (talk | contribs) No edit summary |
Paola Ariza (talk | contribs) No edit summary |
||
| Line 24: | Line 24: | ||
==== ''Disulfide bonds'' ==== | ==== ''Disulfide bonds'' ==== | ||
In common Class A GPCRs the disulfide bond associated with the initiation of signal transduction is located on the extracellular domain of the 7 transmembrane helices. <ref name="Zhang">PMID: 26467290</ref> The <scene name='90/904327/B2ardisulfidebond1_pt_3/1'>disulfide bond of β2AR </scene>, a well studied Class A GPCR, occurs between transmembrane three (TM3) C106 and extracellular loop (EL) C191. This loop crosses through the middle of the extracellular domain, creating a barrier for bulkier substrates. | In common Class A GPCRs the disulfide bond associated with the initiation of signal transduction is located on the extracellular domain of the 7 transmembrane helices. <ref name="Zhang">PMID: 26467290</ref> The <scene name='90/904327/B2ardisulfidebond1_pt_3/1'>disulfide bond of β2AR </scene>, a well studied Class A GPCR, occurs between transmembrane three (TM3) C106 and extracellular loop (EL) C191. This loop crosses through the middle of the extracellular domain, creating a barrier for bulkier substrates. The <scene name='90/904327/7tm_domain_pt_6/1'>disulfide bond of MRGPRX2</scene> is located between (TM4) C168 and (TM5) C180. This is a TM to TM disulfide bond as compared to a TM to EL disulfide bond seen in typical Class A GPCRs. This lack of interaction with the extracellular loop seen in MRGPRX2 causes the extracellular loop to flip on top of the TM4 and TM5 resulting in an open space for larger substrates to be able to interact with the receptor. | ||
==== ''PIF Motif'' ==== | ==== ''PIF Motif'' ==== | ||