| pubmed-article:20351100 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C0013352 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1149274 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20351100 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20351100 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:20351100 | pubmed:dateCreated | 2010-5-17 | lld:pubmed |
| pubmed-article:20351100 | pubmed:abstractText | Dynein interacts with microtubules through a dedicated binding domain that is dynamically controlled to achieve high or low affinity, depending on the state of nucleotide bound in a distant catalytic pocket. The active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a approximately 10-nm length antiparallel coiled-coil stalk, which connects the binding domain to the roughly 300-kDa motor core. Recently, an x-ray structure of the murine cytoplasmic dynein microtubule binding domain (MTBD) in a weak affinity conformation was published, containing a covalently constrained beta(+) registry for the coiled-coil stalk segment (Carter, A. P., Garbarino, J. E., Wilson-Kubalek, E. M., Shipley, W. E., Cho, C., Milligan, R. A., Vale, R. D., and Gibbons, I. R. (2008) Science 322, 1691-1695). We here present an NMR analysis of the isolated MTBD from Dictyostelium discoideum that demonstrates the coiled-coil beta(+) registry corresponds to the low energy conformation for this functional region of dynein. Addition of sequence encoding roughly half of the coiled-coil stalk proximal to the binding tip results in a decreased affinity of the MTBD for microtubules. In contrast, addition of the complete coiled-coil sequence drives the MTBD to the conformationally unstable, high affinity binding state. These results suggest a thermodynamic coupling between conformational free energy differences in the alpha and beta(+) registries of the coiled-coil stalk that acts as a switch between high and low affinity conformations of the MTBD. A balancing of opposing conformations in the stalk and MTBD enables potentially modest long-range interactions arising from ATP binding in the motor core to induce a relaxation of the MTBD into the stable low affinity state. | lld:pubmed |
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| pubmed-article:20351100 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20351100 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20351100 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20351100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20351100 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20351100 | pubmed:month | May | lld:pubmed |
| pubmed-article:20351100 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20351100 | pubmed:author | pubmed-author:McNaughtonLyn... | lld:pubmed |
| pubmed-article:20351100 | pubmed:author | pubmed-author:LeMasterDavid... | lld:pubmed |
| pubmed-article:20351100 | pubmed:author | pubmed-author:BanavaliNiles... | lld:pubmed |
| pubmed-article:20351100 | pubmed:author | pubmed-author:KoonceMichael... | lld:pubmed |
| pubmed-article:20351100 | pubmed:author | pubmed-author:TikhonenkoIri... | lld:pubmed |
| pubmed-article:20351100 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20351100 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:20351100 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20351100 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20351100 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20351100 | pubmed:pagination | 15994-6002 | lld:pubmed |
| pubmed-article:20351100 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:meshHeading | pubmed-meshheading:20351100... | lld:pubmed |
| pubmed-article:20351100 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20351100 | pubmed:articleTitle | A low affinity ground state conformation for the Dynein microtubule binding domain. | lld:pubmed |
| pubmed-article:20351100 | pubmed:affiliation | Division of Translational Medicine, Wadsworth Center, Albany, New York 12201-0509, USA. | lld:pubmed |
| pubmed-article:20351100 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20351100 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:20351100 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
