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- W1554145557 endingPage "II" @default.
- W1554145557 startingPage "87" @default.
- W1554145557 abstract "This chapter summarizes the current knowledge of the structure and mechanisms of kinesin and selected other members of this superfamily, focusing on the way ATPase action is coupled to the generation of motility in its various forms. The nomenclature of the kinesin family is confusing. The founding member is the most studied and is often referred to as “conventional kinesin” or as “KHC” and “KLC” for the heavy and light chains, respectively. However, it is also known by the names “KIF5” (a, b, or c) for the three isoforms in mouse and as “kinesin-I,” which unfortunately does not correspond to the designation of the corresponding conventional dimeric myosin as myosin II. The nucleus of conventional kinesin is a dimer of heavy or α-chains of ∼ 1000 amino acid residues that form an extended coiled coil over much of their length. The globular motor domains (the heads) are located at the N-terminus. A broad functional distinction can be made among N-terminal motors, such as conventional kinesin with a variety of cargoes including vesicular ones; the C-terminal motors, which are unique in that they are the only ones to move toward the minus end of the microtubule (MT); and M-kinesins, which can depolymerize MTs and may not have motility as their principal role. All kinesin superfamily members share sequence similarity in the motor domain by definition, but the individual families represent the clusters of higher similarity among themselves, including the insertions and deletions in loop regions. Also the similarity within a family often extends to the nonmotor sequences." @default.
- W1554145557 created "2016-06-24" @default.
- W1554145557 creator A5000308991 @default.
- W1554145557 date "2003-01-01" @default.
- W1554145557 modified "2023-09-25" @default.
- W1554145557 title "Motor proteins of the kinesin superfamily" @default.
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