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| Content Provider | PubMed Central |
|---|---|
| Author | Jha, Archana Auerbach, Anthony |
| Copyright Year | 2010 |
| Abstract | The neuromuscular acetylcholine receptor (AChR) is an allosteric protein that alternatively adopts inactive versus active conformations (R↔R∗ ). The R∗ shape has a higher agonist affinity and ionic conductance than R. To understand how agonists trigger this gating isomerization, we examined single-channel currents from adult mouse muscle AChRs that isomerize normally without agonists but have only a single site able to use agonist binding energy to motivate gating. We estimated the monoliganded gating equilibrium constant E 1 and the energy change associated with the R versus R∗ change in affinity for agonists. AChRs with only one operational binding site gave rise to a single population of currents, indicating that the two transmitter binding sites have approximately the same affinity for the transmitter ACh. The results indicated that E 1 ≈ 4.3 × 10−3 with ACh, and ≈1.7 × 10−4 with the partial-agonist choline. From these values and the diliganded gating equilibrium constants, we estimate that the unliganded AChR gating constant is E 0 ≈ 6.5 × 10−7. Gating changes the stability of the ligand-protein complex by ∼5.2 kcal/mol for ACh and ∼3.3 kcal/mol for choline. |
| Related Links | http://dx.doi.org/10.1016/j.bpj.2010.01.025 |
| Ending Page | 1846 |
| Page Count | 7 |
| Starting Page | 1840 |
| File Format | |
| ISSN | 00063495 |
| e-ISSN | 15420086 |
| Journal | Biophysical Journal |
| Issue Number | 9 |
| Volume Number | 98 |
| Language | English |
| Publisher | The Biophysical Society |
| Publisher Date | 2010-05-01 |
| Access Restriction | Open |
| Rights Holder | The Biophysical Society |
| Subject Keyword | Biophysics Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biophysics |
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