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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2002-8-7
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pubmed:abstractText |
Voltage-dependent L-type Ca(2+) channels play important functional roles in many excitable cells. We present a three-dimensional structure of an L-type Ca(2+) channel. Electron cryomicroscopy in conjunction with single-particle processing was used to determine a 30-A resolution structure of the channel protein. The asymmetrical channel structure consists of two major regions: a heart-shaped region connected at its widest end with a handle-shaped region. A molecular model is proposed for the arrangement of this skeletal muscle L-type Ca(2+) channel structure with respect to the sarcoplasmic reticulum Ca(2+)-release channel, the physical partner of the L-type channel for signal transduction during the excitation-contraction coupling in muscle.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-10419512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-10512814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-10600563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-10790202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-11031246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-11234014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-11264005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-11500484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-1648106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-1847144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2165570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2450086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2454049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2455723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2458626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2469159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2558713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2641949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2826471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2849609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-2853487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-3043536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-6386826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7516685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7560004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7574491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7673188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7719847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-7742348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-8120002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-8134386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-8171118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-8598910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-9151688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-9176137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-9593671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12149473-9792715
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pubmed:keyword |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10370-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
Structure of the voltage-gated L-type Ca2+ channel by electron cryomicroscopy.
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pubmed:affiliation |
Department of Molecular Physiology and Biophysics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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