| pubmed-article:12169104 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C0667268 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1823153 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C2349976 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1552644 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:12169104 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:12169104 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12169104 | pubmed:dateCreated | 2002-8-9 | lld:pubmed |
| pubmed-article:12169104 | pubmed:abstractText | We have modelled the conformation of the III-IV loop of the Ca(v)2.1 subunit of P/Q calcium channels, a loop that is implicated in fast voltage-dependent inactivation. Change in channel inactivation requires its direct interaction with the I-II loop. This interaction occurs with an affinity in the order of 70 nm. Intracellular injection of a 40-mer III-IV loop-derived peptide produces an increase in the rate of fast inactivation. This alteration in channel kinetic is also accompanied by a hyperpolarizing shift in the steady-state voltage-dependence of inactivation. None of these effects are observed in the presence of a beta subunit, suggesting the existence of a competitive mechanism of action between the beta subunit and the III-IV loop. Amino acid sequence comparison using BLAST reveals that the III-IV loop shares 53% identity with the gamma subunit of G proteins. Because of the pivotal contribution of the III-IV loop to inactivation, an atomic model of the III-IV loop was generated by both homology modelling and molecular mechanics calculations. Using the X-ray structures of the betagamma dimer of the heterotrimeric G-proteins as templates, the III-IV loop is predicted to contain a well-structured alpha-helix at the amino-terminus with both the N- and C-termini having the same orientation in the plane of the inner lipid bilayer. We provide a hypothetical working model in which we propose that the III-IV loop interacts with the I-II loop via its Gbetagamma binding domain. | lld:pubmed |
| pubmed-article:12169104 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12169104 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12169104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169104 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12169104 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12169104 | pubmed:issn | 0953-816X | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:GeibSandrineS | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:VillazMichelM | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:RonjatMichelM | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:SandozGuillau... | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:SabatierJean-... | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:MabroukKamelK | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:FathallahMoha... | lld:pubmed |
| pubmed-article:12169104 | pubmed:author | pubmed-author:UrbaniJulieJ | lld:pubmed |
| pubmed-article:12169104 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12169104 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:12169104 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12169104 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12169104 | pubmed:pagination | 219-28 | lld:pubmed |
| pubmed-article:12169104 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12169104 | pubmed:meshHeading | pubmed-meshheading:12169104... | lld:pubmed |
| pubmed-article:12169104 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12169104 | pubmed:articleTitle | Modelling of the III-IV loop, a domain involved in calcium channel Ca(v)2.1 inactivation, highlights a structural homology with the gamma subunit of G proteins. | lld:pubmed |
| pubmed-article:12169104 | pubmed:affiliation | Laboratoire de Biochimie, CNRS UMR 6560, Faculté de Médecine Nord, Boulevard Pierre Dramard, 13916 Marseille Cedex 20, France. | lld:pubmed |
| pubmed-article:12169104 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12169104 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12169104 | lld:pubmed |
