1byw
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1byw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byw OCA], [http://www.ebi.ac.uk/pdbsum/1byw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1byw RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function. | The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Lathosterolosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602286 602286]], Long QT syndrome, acquired, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=152427 152427]], Long QT syndrome-2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=152427 152427]], Short QT syndrome-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=152427 152427]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: potassium channel domain]] | [[Category: potassium channel domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:11:14 2008'' |
Revision as of 16:11, 30 March 2008
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| , resolution 2.6Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL
Overview
The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function.
About this Structure
1BYW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain., Morais Cabral JH, Lee A, Cohen SL, Chait BT, Li M, Mackinnon R, Cell. 1998 Nov 25;95(5):649-55. PMID:9845367
Page seeded by OCA on Sun Mar 30 19:11:14 2008
