| pubmed-article:16030013 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1180334 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1947953 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1514721 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1149666 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C2700372 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16030013 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:16030013 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:16030013 | pubmed:dateCreated | 2005-9-19 | lld:pubmed |
| pubmed-article:16030013 | pubmed:abstractText | The dynein motor domain consists of a ring of six AAA domains with a protruding microtubule-binding stalk and a C-terminal domain of unknown function. To understand how conformational information is communicated within this complex structure, we produced a series of recombinant and proteolytic rat motor domain fragments, which we analyzed enzymatically. A recombinant 210-kDa half-motor domain fragment surprisingly exhibited a 6-fold higher steady state ATPase activity than a 380-kDa complete motor domain fragment. The increased ATPase activity was associated with a complete loss of sensitivity to inhibition by vanadate and an approximately 100-fold increase in the rate of ADP release. The time course of product release was discovered to be biphasic, and each phase was stimulated approximately 1000-fold by microtubule binding to the 380-kDa motor domain. Both the half-motor and full motor domain fragments were remarkably resistant to tryptic proteolysis, exhibiting either two or three major cleavage sites. Cleavage near the C terminus of the 380-kDa motor domain released a 32-kDa fragment and abolished sensitivity to vanadate. Cleavage at this site was insensitive to ATP or 5'-adenylyl-beta,gamma-imidodiphosphate but was blocked by ADP-AlF3 or ADP-vanadate. Based on these data, we proposed a model for long range allosteric control of product release at AAA1 and AAA3 through the microtubule-binding stalk and the C-terminal domain, the latter of which may interact with AAA1 to close the motor domain ring in a cross-bridge cycle-dependent manner. | lld:pubmed |
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| pubmed-article:16030013 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16030013 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16030013 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16030013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16030013 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16030013 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16030013 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:ChaitBrian... | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:ValleeRichard... | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:MikamiAtsushi... | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:RosenfeldStev... | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:HöökPeterP | lld:pubmed |
| pubmed-article:16030013 | pubmed:author | pubmed-author:ShaferBethB | lld:pubmed |
| pubmed-article:16030013 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16030013 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:16030013 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:16030013 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16030013 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16030013 | pubmed:pagination | 33045-54 | lld:pubmed |
| pubmed-article:16030013 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16030013 | pubmed:meshHeading | pubmed-meshheading:16030013... | lld:pubmed |
| pubmed-article:16030013 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16030013 | pubmed:articleTitle | Long range allosteric control of cytoplasmic dynein ATPase activity by the stalk and C-terminal domains. | lld:pubmed |
| pubmed-article:16030013 | pubmed:affiliation | Department of Pathology and Cell Biology, Columbia University, New York, New York 10032, USA. | lld:pubmed |
| pubmed-article:16030013 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16030013 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16030013 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16030013 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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