http://purl.uniprot.org/citations/12754210 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12754210 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12754210 | http://www.w3.org/2000/01/rdf-schema#comment | "Voltage-gated potassium channels are formed by the tetramerization of their alpha subunits, in a process that is controlled by their conserved N-terminal T1 domains. The crystal structures of Shaker and Shaw T1 domains reveal interesting differences in structures that are contained within a highly conserved BTB/POZ domain fold. The most surprising difference is that the Shaw T1 domain contains an intersubunit Zn2+ ion that is lacking in the Shaker T1 domain. The Zn2+ coordination motif is conserved in other non-Shaker channels making this the most distinctive difference between these channels and Shaker. In this study we show that Zn2+ is an important co-factor for the tetramerization of isolated Shaw and Shal T1 domains. Addition of Zn2+ increases the amount of tetramer formed, whereas chelation of Zn2+ with phenanthroline blocks tetramerization and causes assembled tetramers to disassemble. Within an intact cell, full-length Shal subunits containing Zn2+ site mutations also fail to form functional channels, with the majority of the protein found to remain monomeric by size exclusion chromatography. Therefore, zinc-mediated tetramerization also is a physiologically important event for full-length functional channel formation."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m304268200"xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m304268200"xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Kunjilwar K."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Kunjilwar K."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Peterson D."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Peterson D."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "DeRubeis D."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "DeRubeis D."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Pfaffinger P.J."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Pfaffinger P.J."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Strang C."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/author | "Strang C."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/pages | "31361-31371"xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/pages | "31361-31371"xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/title | "The role of Zn2+ in Shal voltage-gated potassium channel formation."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/title | "The role of Zn2+ in Shal voltage-gated potassium channel formation."xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/volume | "278"xsd:string |
http://purl.uniprot.org/citations/12754210 | http://purl.uniprot.org/core/volume | "278"xsd:string |