Ion channel structures: a review of recent progress.
Several ion channel structures have recently been determined, including MthK (a bacterial K+ channel in an open state), KirBac (a bacterial homolog of mammalian inward rectifier K+ channels), KvAP (a bacterial voltage-activated K+ channel) and the pore domain of the nicotinic acetylcholine receptor....
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2003
|
| _version_ | 1826292570546765824 |
|---|---|
| author | Domene, C Haider, S Sansom, MS |
| author_facet | Domene, C Haider, S Sansom, MS |
| author_sort | Domene, C |
| collection | OXFORD |
| description | Several ion channel structures have recently been determined, including MthK (a bacterial K+ channel in an open state), KirBac (a bacterial homolog of mammalian inward rectifier K+ channels), KvAP (a bacterial voltage-activated K+ channel) and the pore domain of the nicotinic acetylcholine receptor. Analysis of these structures has increased our understanding of the molecular mechanisms underlying channel gating. A hydrophobic gate appears to operate in a number of channels. Structures of ligand binding domains provide some clues as to how ligand-induced conformational changes control channel gating, but further experimental and computational studies are required before a full picture emerges. |
| first_indexed | 2024-03-07T03:16:44Z |
| format | Journal article |
| id | oxford-uuid:b6081fcc-f890-4d95-9b77-b96a791119da |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:16:44Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:b6081fcc-f890-4d95-9b77-b96a791119da2022-03-27T04:38:07ZIon channel structures: a review of recent progress.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b6081fcc-f890-4d95-9b77-b96a791119daEnglishSymplectic Elements at Oxford2003Domene, CHaider, SSansom, MSSeveral ion channel structures have recently been determined, including MthK (a bacterial K+ channel in an open state), KirBac (a bacterial homolog of mammalian inward rectifier K+ channels), KvAP (a bacterial voltage-activated K+ channel) and the pore domain of the nicotinic acetylcholine receptor. Analysis of these structures has increased our understanding of the molecular mechanisms underlying channel gating. A hydrophobic gate appears to operate in a number of channels. Structures of ligand binding domains provide some clues as to how ligand-induced conformational changes control channel gating, but further experimental and computational studies are required before a full picture emerges. |
| spellingShingle | Domene, C Haider, S Sansom, MS Ion channel structures: a review of recent progress. |
| title | Ion channel structures: a review of recent progress. |
| title_full | Ion channel structures: a review of recent progress. |
| title_fullStr | Ion channel structures: a review of recent progress. |
| title_full_unstemmed | Ion channel structures: a review of recent progress. |
| title_short | Ion channel structures: a review of recent progress. |
| title_sort | ion channel structures a review of recent progress |
| work_keys_str_mv | AT domenec ionchannelstructuresareviewofrecentprogress AT haiders ionchannelstructuresareviewofrecentprogress AT sansomms ionchannelstructuresareviewofrecentprogress |