Structural and Thermodynamic Basis of the Enhanced Interaction between Kinesin Spindle Protein Eg5 and STLC-type Inhibitors

[Image: see text] For a better understanding of protein–inhibitor interactions, we report structural, thermodynamic, and biological analyses of the interactions between S-trityl-l-cysteine (STLC) derivatives and the motor domain of kinesin spindle protein Eg5. Binding of STLC-type inhibitors to Eg5...

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Detalles Bibliográficos
Autores principales: Yokoyama, Hideshi, Sawada, Jun-ichi, Sato, Kohei, Ogo, Naohisa, Kamei, Nanami, Ishikawa, Yoshinobu, Hara, Kodai, Asai, Akira, Hashimoto, Hiroshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6644766/
https://www.ncbi.nlm.nih.gov/pubmed/31459302
http://dx.doi.org/10.1021/acsomega.8b00778

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6644766/
https://www.ncbi.nlm.nih.gov/pubmed/31459302
http://dx.doi.org/10.1021/acsomega.8b00778

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