4hna | pdb_00004hna
From Proteopedia
Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN
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Structural highlights
Function[KINH_HUMAN] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity). Publication Abstract from PubMedThe typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to alphabeta-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken. Structure of a kinesin-tubulin complex and implications for kinesin motility.,Gigant B, Wang W, Dreier B, Jiang Q, Pecqueur L, Pluckthun A, Wang C, Knossow M Nat Struct Mol Biol. 2013 Aug;20(8):1001-7. doi: 10.1038/nsmb.2624. Epub 2013 Jul, 21. PMID:23872990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 03:18, 25 December 2014.