3ZCW
Eg5 - New allosteric binding site
Summary for 3ZCW
| Entry DOI | 10.2210/pdb3zcw/pdb |
| Descriptor | KINESIN-LIKE PROTEIN KIF11, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | cell cycle, inhibitor |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm: P52732 |
| Total number of polymer chains | 1 |
| Total formula weight | 40521.78 |
| Authors | Ulaganathan, V.,Talapatra, S.K.,Kozielski, F.,Pannifer, A.D. (deposition date: 2012-11-23, release date: 2013-01-23, Last modification date: 2023-12-20) |
| Primary citation | Ulaganathan, V.,Talapatra, S.K.,Rath, O.,Pannifer, A.D.,Hackney, D.D.,Kozielski, F. Structural Insights Into a Unique Inhibitor Binding Pocket in Kinesin Spindle Protein. J.Am.Chem.Soc., 135:2263-, 2013 Cited by PubMed Abstract: Human kinesin Eg5 is a target for drug development in cancer chemotherapy with compounds in phase II clinical trials. These agents bind to a well-characterized allosteric pocket involving the loop L5 region, a structural element in kinesin-5 family members thought to provide inhibitor specificity. Using X-ray crystallography, kinetic, and biophysical methods, we have identified and characterized a distinct allosteric pocket in Eg5 able to bind inhibitors with nanomolar K(d). This pocket is formed by key structural elements thought to be pivotal for force generation in kinesins and may represent a novel site for therapeutic intervention in this increasingly well-validated drug target. PubMed: 23305346DOI: 10.1021/JA310377D PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.691 Å) |
Structure validation
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