Family-specific Kinesin Structures Reveal Neck-linker Length Based on Initiation of the Coiled-coil

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Family-specific Kinesin Structures Reveal Neck-linker Length Based on Initiation of the Coiled-coil.

Kinesin-1, -2, -5, and -7 generate processive hand-over-hand 8-nm steps to transport intracellular cargoes toward the microtubule plus end. This processive motility requires gating mechanisms to coordinate the mechanochemical cycles of the two motor heads to sustain the processive run. A key structural element believed to regulate the degree of processivity is the neck-linker, a short peptide o...

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The coiled-coil helix in the neck of kinesin.

Kinesin is a microtubule-dependent motor protein. We have recently determined the X-ray structure of monomeric and dimeric kinesin from rat brain. The dimer consists of two motor domains, held together by their alpha-helical neck domains forming a coiled coil. Here we analyze the nature of the interactions in the neck domain (residues 339-370). Overall, the neck helix shows a heptad repeat (abc...

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Neck Linker Length Determines the Degree of Processivity in Kinesin-1 and Kinesin-2 Motors

Defining the mechanical and biochemical determinates of kinesin processivity is important for understanding how diverse kinesins are tuned for specific cellular functions. Because transmission of mechanical forces through the 14-18 amino acid neck linker domain underlies coordinated stepping, we investigated the role of neck linker length, charge, and structure in kinesin-1 and kinesin-2 motor ...

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Neck Linker Length Determin

Defining the mechanical and biochemical determinates of kinesin processivity is important for understanding how diverse kinesins are tuned for specific cellular functions. Because transmission of mechanical forces through the 14–18 amino acid neck linker domain underlies coordinated stepping [1–6], we investigated the role of neck linker length, charge, and structure in kinesin-1 and kinesin-2 ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2016

ISSN: 0021-9258

DOI: 10.1074/jbc.m116.737577