1T5C

Crystal structure of the motor domain of human kinetochore protein CENP-E

1T5C の概要

• エントリーDOI: 10.2210/pdb1t5c/pdb
• 分子名称: Centromeric protein E, MAGNESIUM ION, NITRATE ION, ... (6 entities in total)
• 機能のキーワード: kinesin motor-domain-adp complex, stranded beta-sheet core with solvent exposed alpha-helices, arrow-head shape, structural proteomics in europe, spine, structural genomics, contractile protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79938.18

構造登録者

Garcia-Saez, I.,Yen, T.,Wade, R.H.,Kozielski, F.,Structural Proteomics in Europe (SPINE) (登録日: 2004-05-04, 公開日: 2005-05-10, 最終更新日: 2023-08-23)

主引用文献

Garcia-Saez, I.,Yen, T.,Wade, R.H.,Kozielski, F.
Crystal structure of the motor domain of the human kinetochore protein CENP-E.
J.Mol.Biol., 340:1107-1116, 2004

PubMed Abstract: The human kinetochore is a highly complex macromolecular structure that connects chromosomes to spindle microtubules (MTs) in order to facilitate accurate chromosome segregation. Centromere-associated protein E (CENP-E), a member of the kinesin superfamily, is an essential component of the kinetochore, since it is required to stabilize the attachment of chromosomes to spindle MTs, to develop tension across aligned chromosomes, to stabilize spindle poles and to satisfy the mitotic checkpoint. Here we report the 2.5A resolution crystal structure of the motor domain and linker region of human CENP-E with MgADP bound in the active site. This structure displays subtle but important differences compared to the structures of human Eg5 and conventional kinesin. Our structure reveals that the CENP-E linker region is in a "docked" position identical to that in the human plus-end directed conventional kinesin. CENP-E has many advantages as a potential anti-mitotic drug target and this crystal structure of human CENP-E will provide a starting point for high throughput virtual screening of potential inhibitors.

PubMed: 15236970
DOI: 10.1016/j.jmb.2004.05.053

実験手法

X-RAY DIFFRACTION (2.5 Å)