Kinesin, 30 years later: Recent insights from structural studies

• Published in: Protein science Vol. 24; no. 7; pp. 1047 - 1056
• Main Authors: Wang, Weiyi, Cao, Luyan, Wang, Chunguang, Gigant, Benoît, Knossow, Marcel
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.07.2015; Wiley; John Wiley & Sons, Ltd
• Subjects: Adenosine Triphosphate; Adenosine Triphosphate - metabolism; Animals; ATP; Biochemistry, Molecular Biology; Cryoelectron Microscopy; Crystallography; Crystallography, X-Ray; Docking; Electron microscopy; Humans; Kinesin; Kinesin - antagonists & inhibitors; Kinesin - chemistry; Kinesin - metabolism; Life Sciences; mechanism; Microtubules; Models, Molecular; Molecular motors; motor protein; myosin; Myosins; Myosins - metabolism; processivity; Protein Conformation; Proteins; Reviews; Structural Biology; structure; Tubulin; Tubulin - metabolism; myosin; microtubules; mechanism; processivity; motor protein; structure
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1002/pro.2697

Motile kinesins are motor proteins that move unidirectionally along microtubules as they hydrolyze ATP. They share a conserved motor domain (head) which harbors both the ATP‐ and microtubule‐binding activities. The kinesin that has been studied most moves toward the microtubule (+)‐end by alternatel...