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首页> 外文期刊>Biochemistry >Structure of the Plasminogen Kringle 4 Binding Calcium-Free Form of the C-Type Lectin-Like Domain of Tetranectin
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Structure of the Plasminogen Kringle 4 Binding Calcium-Free Form of the C-Type Lectin-Like Domain of Tetranectin

机译:纤溶酶C型凝集素样结构域的纤溶酶Kringle 4结合无钙形式。

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摘要

Tetranectin is a homotrimeric protein containing a C-type lectin-like domain.This domain (TN3) can bind calcium,but in the absence of calcium,the domain binds a number of kringle-type protein ligands.Two of the calcium-coordinating residues are also critical for binding plasminogen kringle 4 (K4).The structure of the calcium free-form of TN3 (apoTN3) has been determined by NMR.Compared to the structure of the calcium-bound form of TN3 (holoTN3),the core region of secondary structural elements is conserved,while large displacements occur in the loops involved in calcium or K4 binding.A conserved proline,which was found to be in the cis conformation in holoTN3,is in apoTN3 predominantly in the trans conformation.Backbone dynamics indicate that,in apoTN3 especially,two of the three calcium-binding loops and two of the three K4-binding residues exhibit increased flexibility,whereas no such flexibility is observed in holoTN3.In the 20 best nuclear magnetic resonance structures of apoTN3,the residues critical for K4 binding span a large conformational space.Together with the relaxation data,this indicates that the K4-ligand-binding site in apoTN3 is not preformed.
机译:Tetranectin是含有C型凝集素样结构域的同源三聚体蛋白。该结构域(TN3)可以结合钙,但在没有钙的情况下,该结构域结合许多kringle型蛋白质配体。两个钙配位残基TN3(apoTN3)的钙游离形式的结构已通过NMR确定。与TN3(holoTN3)的钙结合形式的结构相比,核心区域二级结构元素被保守,而钙或K4结合所涉及的环中发生大位移。被发现的保守脯氨酸在holoTN3中呈顺式构象,而在apoTN3中则主要处于反式构象。骨动力学表明特别是在apoTN3中,三个钙结合环中的两个和三个与K4结合的残基中的两个表现出增加的柔性,而在holoTN3中未观察到这种柔性。在apoTN3的20种最佳核磁共振结构中,与K4结合至关重要的残基跨越一个大的构象空间。再加上弛豫数据,这表明apoTN3中的K4-配体结合位点尚未形成。

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