8HFH

CENP-E motor domain in complex with AMPPNP and Mg2+

Summary for 8HFH

• Entry DOI: 10.2210/pdb8hfh/pdb
• Related: 6M4I
• Descriptor: Centromere-associated protein E, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: kinesin, motor domain, amppnp, cenp-e, centromere-associated protein, cell cycle
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 40467.64

Authors

Shibuya, A.,Yokoyama, H. (deposition date: 2022-11-10, release date: 2023-03-08, Last modification date: 2023-11-29)

Primary citation

Shibuya, A.,Suzuki, A.,Ogo, N.,Sawada, J.I.,Asai, A.,Yokoyama, H.
Crystal structure of the motor domain of centromere-associated protein E in complex with a non-hydrolysable ATP analogue.
Febs Lett., 597:1138-1148, 2023

PubMed Abstract: Centromere-associated protein E (CENP-E) is a kinesin motor protein essential for mitosis and a new target for anticancer agents with less side effects. To rationally design anticancer drug candidates based on structure, it is important to determine the three-dimensional structure of the CENP-E motor domain bound to its inhibitor. Here, we report the first crystal structure of the CENP-E motor domain in complex with a non-hydrolysable ATP analogue, adenylyl-imidodiphosphate (AMPPNP). Furthermore, the structure is compared with the ADP-bound form of the CENP-E motor domain as well as the AMPPNP-bound forms of other kinesins. This study indicates that helix α4 of CENP-E participates in the slow binding of CENP-E to microtubules. These results will contribute to the development of anticancer drugs targeting CENP-E.

PubMed: 36823439
DOI: 10.1002/1873-3468.14602

Experimental method

X-RAY DIFFRACTION (1.8 Å)