| pubmed-article:11136855 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C1325742 | lld:lifeskim |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C0032824 | lld:lifeskim |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:11136855 | lifeskim:mentions | umls-concept:C0964377 | lld:lifeskim |
| pubmed-article:11136855 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:11136855 | pubmed:dateCreated | 2001-1-26 | lld:pubmed |
| pubmed-article:11136855 | pubmed:abstractText | Cells maintain a negative resting membrane potential through the constitutive activity of background K+ channels. A novel multigene family of such K+ channels has recently been identified. A unique characteristic of these K+ channels is the presence of two homologous, subunit-like domains, each containing a pore-forming region. Sequence co-variations in the GYGD signature motifs of the two pore regions suggested an interaction between neighbouring pore domains. Mutations of the GYGD motif in the rat drk1 (Kv2.1) K+ channel showed that the tyrosine (Y) position was important for K+ selectivity and single channel conductance, whereas the aspartate (D) position was a critical determinant of open state stability. Tandem constructs engineered to mimic the GYGx-GxGD pattern seen in two-domain K+ channels delineated a co-operative intersubunit interaction between the Y and D positions, which determined ion selectivity, conductance and gating. In the bacterial KcsA K+ channel crystal structure, the equivalent aspartate residue (D80) does not directly interact with permeating K+ ions. However, the data presented here show that the D position is able to fine-tune ion selectivity through a functional interaction with the Y position in the neighbouring subunit. These data indicate a physiological basis for the extensive sequence variation seen in the GYGD motifs of two-domain K+ channels. It is suggested that a cell can precisely regulate its resting membrane potential by selectively expressing a complement of two-domain K+ channels. | lld:pubmed |
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| pubmed-article:11136855 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11136855 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11136855 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11136855 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11136855 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11136855 | pubmed:issn | 0022-3751 | lld:pubmed |
| pubmed-article:11136855 | pubmed:author | pubmed-author:ChapmanM LML | lld:pubmed |
| pubmed-article:11136855 | pubmed:author | pubmed-author:VanDongenA... | lld:pubmed |
| pubmed-article:11136855 | pubmed:author | pubmed-author:KrovetzH SHS | lld:pubmed |
| pubmed-article:11136855 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11136855 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11136855 | pubmed:volume | 530 | lld:pubmed |
| pubmed-article:11136855 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11136855 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11136855 | pubmed:pagination | 21-33 | lld:pubmed |
| pubmed-article:11136855 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11136855 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11136855 | pubmed:articleTitle | GYGD pore motifs in neighbouring potassium channel subunits interact to determine ion selectivity. | lld:pubmed |
| pubmed-article:11136855 | pubmed:affiliation | Department of Pharmacology and Cancer Biology, Duke University Medical Center, PO Box 3813, Durham, NC 27708, USA. | lld:pubmed |
| pubmed-article:11136855 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11136855 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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