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The adociasulfate-2 (AS-2) binding regions of two human kinesins, centromere-associated protein E (CENP-E), a member of the kinesin-7 family, the Eg5, a member of the kinesin-5 family and the microtubules (MT)-binding region are investigated. The results have shown that AS-2 is a MT-competitive inhibitor of the human CENP-E motor domain.

Hydrogen-deuterium exchange mass spectrometry is used to identify the secondary structure elements that form the binding sites of new Eg5 inhibitors, in particular for S-trityl-L-cysetine, a potent inhibitor of Eg5 activity in vitro and in cell-based assays. Thus, it is shown that S-trityl-L-cysteine and monastrol both bind to the same region on Eg5 by induced fit in a pocket formed by helix alpha3-strand beta5 and loop L5-helix alpha2.

An EDTA-free protocol was used to determine the crystal structure of periplasmic BTC-Ni-NikA complex synthesized from apo protein and commercial reagents. The results revealed that the novel nickel-free BTC-NikA protein-chelator complex observed in chloroform-extracted NikA crystals might correspond to a natural NikA-Ni-metallophore species.