2KIN

KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS

2KIN の概要

• エントリーDOI: 10.2210/pdb2kin/pdb
• 分子名称: KINESIN, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: motor protein, cytoskeleton
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38958.06

構造登録者

Sack, S.,Muller, J.,Kozielski, F.,Marx, A.,Thormahlen, M.,Biou, V.,Mandelkow, E.-M.,Brady, S.T.,Mandelkow, E. (登録日: 1997-04-28, 公開日: 1998-04-08, 最終更新日: 2024-04-03)

主引用文献

Sack, S.,Muller, J.,Marx, A.,Thormahlen, M.,Mandelkow, E.M.,Brady, S.T.,Mandelkow, E.
X-ray structure of motor and neck domains from rat brain kinesin.
Biochemistry, 36:16155-16165, 1997

PubMed Abstract: We have determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J., et al. (1996) Nature 380, 550-554]. Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al. (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure.

PubMed: 9405049
DOI: 10.1021/bi9722498

実験手法

X-RAY DIFFRACTION (2 Å)