ABCC8 p.Tyr179Trp

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PMID: 21685390 [PubMed] Marquer C et al: "Structural model of ligand-G protein-coupled receptor (GPCR) complex based on experimental double mutant cycle data: MT7 snake toxin bound to dimeric hM1 muscarinic receptor."
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271 This distance is similar to the distance between the two MT7 binding sites centered on Tyr-179/Trp-400 of each protomer in our model of MT7-hM1 dimer complex (Fig. 8B).
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ABCC8 p.Tyr179Trp 21685390:271:87
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277 In this case, the distance between the two MT7 binding sites (Tyr-179/Trp-400) is too large (35 Å) to receive the tips of MT7 loops (Fig. 8C).
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ABCC8 p.Tyr179Trp 21685390:277:62
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280 Fig. 8D shows the variation of the distances between the MT7 binding sites (Tyr-179/Trp-400) of both protomers as a function of the angle of rotation of each protomer around their vertical axis.
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ABCC8 p.Tyr179Trp 21685390:280:76
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283 This is due to the fact that Tyr-179/Trp- FIGURE 5.
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ABCC8 p.Tyr179Trp 21685390:283:29
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336 Therefore, the MT7-hM1 dimer recognition site is composed of three patches on MT7 (the tips of the three loops) and two patches on the hM1 side (the binding sites of the two protomers; Tyr-179/Trp-400), forming a totalinterfaceareaequalto2400Å2 .Thisvalueisclosetothemean valueoftheprotein/proteininterfaceareasreportedfortwo-patch interactions (2500 Å2 ) (73).
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ABCC8 p.Tyr179Trp 21685390:336:185
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350 B, hM1 dimer conformation calculated from our experimental data viewed from the extracellular face (Tyr-179/Trp-400 in green).
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ABCC8 p.Tyr179Trp 21685390:350:100
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351 C, hM1 dimer conformation based on the CXCR4 chemokine structure viewed from the extracellular face (Tyr-179/Trp-400 in yellow).
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ABCC8 p.Tyr179Trp 21685390:351:101
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352 D, measurements of the distancesbetweenthetwocentersofgravityoftheprotomersofthereceptor (E) and the two centers of mass of the MT7 binding sites (Tyr-179/Trp-400) of the protomers (f) during the step by step rotation of each protomer around their vertical axis.
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ABCC8 p.Tyr179Trp 21685390:352:147
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