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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural plasticity of tubulin assembly probed by vinca-domain ligands
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Structural plasticity of tubulin assembly probed by vinca-domain ligands

机译：结构塑性微管蛋白装配了由vinca-domain配体

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摘要

Vinca-domain ligands are compounds that bind to tubulin at its inter-heterodimeric interface and favour heterogeneous protofilament-like assemblies, giving rise to helices and rings. This is the basis for their inhibition of microtubule assembly, for their antimitotic activities and for their use in anticancer chemotherapy. Ustiloxins are vinca-domain ligands with a well established total synthesis. A 2.7 ? resolution structure of ustiloxin D bound to the vinca domain embedded in the complex of two tubulins with the stathmin-like domain of RB3 (T2R) has been determined. This finding precisely defines the interactions of ustiloxins with tubulin and, taken together with structures of other vinca-ligand complexes, allows structure-based suggestions to be made for improved activity. These comparisons also provide a rationale for the large-scale polymorphism of the protofilament-like assemblies mediated by vinca-domain ligands based on local differences in their interactions with the two tubulin heterodimers constituting their binding site.
机译：Vinca-domain配体化合物结合inter-heterodimeric接口和微管蛋白支持异构protofilament-like总成,螺旋和戒指。这是他们的抑制的基础微管组装、抗有丝分裂的活动和用于抗癌的物质化疗。完善的全合成。决议ustiloxin D绑定到的结构长春花域嵌入到复杂的两种微管蛋白RB3 stathmin-like域(T2R)已经被确定。定义ustiloxins的交互微管蛋白,结合结构其他vinca-ligand复合物,允许基于结构的建议了改善活动。大规模的多态性的理由由protofilament-like集合vinca-domain配体基于局部差异在他们两个微管蛋白的相互作用形成构成他们的结合位点。

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