| pubmed-article:10399921 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10399921 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:10399921 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10399921 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:10399921 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:10399921 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10399921 | pubmed:dateCreated | 1999-7-29 | lld:pubmed |
| pubmed-article:10399921 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10399921 | pubmed:abstractText | The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function of beta subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian beta subunits by X-ray crystallography at 2.8 A resolution. Like the integral membrane component of K+ channels, beta subunits form a four-fold symmetric structure. Each subunit is an oxidoreductase enzyme complete with a nicotinamide co-factor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel's voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell. | lld:pubmed |
| pubmed-article:10399921 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10399921 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10399921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10399921 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10399921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10399921 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10399921 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10399921 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:10399921 | pubmed:author | pubmed-author:MannSS | lld:pubmed |
| pubmed-article:10399921 | pubmed:author | pubmed-author:MacKinnonRR | lld:pubmed |
| pubmed-article:10399921 | pubmed:author | pubmed-author:GulbisJ MJM | lld:pubmed |
| pubmed-article:10399921 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10399921 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10399921 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10399921 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10399921 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10399921 | pubmed:pagination | 943-52 | lld:pubmed |
| pubmed-article:10399921 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10399921 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10399921 | pubmed:articleTitle | Structure of a voltage-dependent K+ channel beta subunit. | lld:pubmed |
| pubmed-article:10399921 | pubmed:affiliation | Laboratory of Molecular Neurobiology and Biophysics and the Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:10399921 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10399921 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10399921 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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