pubmed-article:12426369 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C0038454 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C0085139 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C0032863 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C0205288 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C1705994 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C1513492 | lld:lifeskim |
pubmed-article:12426369 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:12426369 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:12426369 | pubmed:dateCreated | 2002-11-11 | lld:pubmed |
pubmed-article:12426369 | pubmed:abstractText | We used cryo-electron microscopy and image reconstruction to investigate the structure and microtubule-binding configurations of dimeric non-claret disjunctional (ncd) motor domains under various nucleotide conditions, and applied molecular docking using ncd's dimeric X-ray structure to generate a mechanistic model for force transduction. To visualize the alpha-helical coiled-coil neck better, we engineered an SH3 domain to the N-terminal end of our ncd construct (296-700). Ncd exhibits strikingly different nucleotide-dependent three-dimensional conformations and microtubule-binding patterns from those of conventional kinesin. In the absence of nucleotide, the neck adapts a configuration close to that found in the X-ray structure with stable interactions between the neck and motor core domain. Minus-end-directed movement is based mainly on two key events: (i) the stable neck-core interactions in ncd generate a binding geometry between motor and microtubule which places the motor ahead of its cargo in the minus-end direction; and (ii) after the uptake of ATP, the two heads rearrange their position relative to each other in a way that promotes a swing of the neck in the minus-end direction. | lld:pubmed |
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pubmed-article:12426369 | pubmed:language | eng | lld:pubmed |
pubmed-article:12426369 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12426369 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12426369 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12426369 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12426369 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12426369 | pubmed:month | Nov | lld:pubmed |
pubmed-article:12426369 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:MüllerJensJ | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:GoldieKenneth... | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:HoengerAndrea... | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:WendtThomas... | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:VolkmannNiels... | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:MandelkowEckh... | lld:pubmed |
pubmed-article:12426369 | pubmed:author | pubmed-author:SkiniotisGeor... | lld:pubmed |
pubmed-article:12426369 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12426369 | pubmed:day | 15 | lld:pubmed |
pubmed-article:12426369 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:12426369 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12426369 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12426369 | pubmed:pagination | 5969-78 | lld:pubmed |
pubmed-article:12426369 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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