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Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathminExpand
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Structural basis for the regulation of tubulin by vinblastine
Vinblastine is one of several tubulin-targeting Vinca alkaloids that have been responsible for many chemotherapeutic successes since their introduction in the clinic as antitumour drugs. In contrastExpand
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Structure of a kinesin–tubulin complex and implications for kinesin motility
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 theExpand
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Variations in the colchicine-binding domain provide insight into the structural switch of tubulin
Structural changes occur in the αβ-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to aExpand
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The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin.
Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to αβ-tubulin is required for microtubule assembly, but whether this triggers conversionExpand
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The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement.
Kinesin-1 is a dimeric ATP-dependent motor protein that moves towards microtubules (+) ends. This movement is driven by two conformations (docked and undocked) of the two motor domainsExpand
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The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex
Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with theExpand
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A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end
Microtubules are cytoskeleton filaments consisting of αβ-tubulin heterodimers. They switch between phases of growth and shrinkage. The underlying mechanism of this property, called dynamicExpand
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The PN2-3 Domain of Centrosomal P4.1-associated Protein Implements a Novel Mechanism for Tubulin Sequestration*
Microtubules are cytoskeletal components involved in multiple cell functions such as mitosis, motility, or intracellular traffic. In vivo, these polymers made of αβ-tubulin nucleate mostly from theExpand
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Structural insight into the inhibition of tubulin by vinca domain peptide ligands
The tubulin vinca domain is the target of widely different microtubule inhibitors that interfere with the binding of vinblastine. Although all these ligands inhibit the hydrolysis of GTP, they affectExpand
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