Structural highlights
4hna is a 4 chain structure with sequence from Human, Ovis aries and Synthetic construct sequences. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Gene: | KIF5B, KNS, KNS1 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[KINH_HUMAN] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity). [D0VWZ0_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] [D0VWY9_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505]
Publication Abstract from PubMed
The 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.
References
- ↑ Gigant B, Wang W, Dreier B, Jiang Q, Pecqueur L, Pluckthun A, Wang C, Knossow M. Structure of a kinesin-tubulin complex and implications for kinesin motility. Nat Struct Mol Biol. 2013 Aug;20(8):1001-7. doi: 10.1038/nsmb.2624. Epub 2013 Jul, 21. PMID:23872990 doi:10.1038/nsmb.2624
