Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study.
The M2delta peptide self-assembles to form a pentameric bundle of transmembrane alpha-helices that is a model of the pore-lining region of the nicotinic acetylcholine receptor. Long (>15 ns) molecular dynamics simulations of a model of the M2delta(5) bundle in a POPC bilayer have been used to...
| Hoofdauteurs: | , , |
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| Formaat: | Journal article |
| Taal: | English |
| Gepubliceerd in: |
2003
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| _version_ | 1826284568967118848 |
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| author | Law, R Tieleman, D Sansom, MS |
| author_facet | Law, R Tieleman, D Sansom, MS |
| author_sort | Law, R |
| collection | OXFORD |
| description | The M2delta peptide self-assembles to form a pentameric bundle of transmembrane alpha-helices that is a model of the pore-lining region of the nicotinic acetylcholine receptor. Long (>15 ns) molecular dynamics simulations of a model of the M2delta(5) bundle in a POPC bilayer have been used to explore the conformational dynamics of the channel assembly. On the timescale of the simulation, the bundle remains relatively stable, with the polar pore-lining side chains remaining exposed to the lumen of the channel. Fluctuations at the helix termini, and in the helix curvature, result in closing/opening transitions at both mouths of the channel, on a timescale of approximately 10 ns. On average, water within the pore lumen diffuses approximately 4x more slowly than water outside the channel. Examination of pore water trajectories reveals both single-file and path-crossing regimes to occur at different times within the simulation. |
| first_indexed | 2024-03-07T01:15:48Z |
| format | Journal article |
| id | oxford-uuid:8e9c5f03-70d6-45b3-ac39-daf1b4ff258f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:15:48Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:8e9c5f03-70d6-45b3-ac39-daf1b4ff258f2022-03-26T22:58:58ZPores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8e9c5f03-70d6-45b3-ac39-daf1b4ff258fEnglishSymplectic Elements at Oxford2003Law, RTieleman, DSansom, MSThe M2delta peptide self-assembles to form a pentameric bundle of transmembrane alpha-helices that is a model of the pore-lining region of the nicotinic acetylcholine receptor. Long (>15 ns) molecular dynamics simulations of a model of the M2delta(5) bundle in a POPC bilayer have been used to explore the conformational dynamics of the channel assembly. On the timescale of the simulation, the bundle remains relatively stable, with the polar pore-lining side chains remaining exposed to the lumen of the channel. Fluctuations at the helix termini, and in the helix curvature, result in closing/opening transitions at both mouths of the channel, on a timescale of approximately 10 ns. On average, water within the pore lumen diffuses approximately 4x more slowly than water outside the channel. Examination of pore water trajectories reveals both single-file and path-crossing regimes to occur at different times within the simulation. |
| spellingShingle | Law, R Tieleman, D Sansom, MS Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title | Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title_full | Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title_fullStr | Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title_full_unstemmed | Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title_short | Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study. |
| title_sort | pores formed by the nicotinic receptor m2delta peptide a molecular dynamics simulation study |
| work_keys_str_mv | AT lawr poresformedbythenicotinicreceptorm2deltapeptideamoleculardynamicssimulationstudy AT tielemand poresformedbythenicotinicreceptorm2deltapeptideamoleculardynamicssimulationstudy AT sansomms poresformedbythenicotinicreceptorm2deltapeptideamoleculardynamicssimulationstudy |