Visualizing a New Binding Site of ncd-Motor Domain on Tubulin
Journal of Structural Biology, ISSN: 1047-8477, Vol: 128, Issue: 1, Page: 26-33
1999
- 8Citations
- 17Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations8
- Citation Indexes8
- CrossRef6
- Captures17
- Readers17
- 17
Article Description
Ncd is a microtubule minus-end directed motor of the kinesin superfamily. Previously it has been shown that ncd and kinesin motor domains share the same major binding site on microtubules. Here we report a three-dimensional EM reconstruction of negatively stained two-dimensional Zn-induced tubulin crystal sheets (Zn-sheets) decorated with the ncd motor domain at a resolution of 16 Å. This work has revealed a second specific binding site for the ncd motor domain. The motor binding site on the tubulin Zn-sheets spans both α and β tubulin subunits. This binding site is located at a position different from the previously identified ncd binding site on microtubules and may play a role in motor function.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S104784779994162X; http://dx.doi.org/10.1006/jsbi.1999.4162; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033386726&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10600555; https://linkinghub.elsevier.com/retrieve/pii/S104784779994162X; https://dx.doi.org/10.1006/jsbi.1999.4162
Elsevier BV
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