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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: A tool to study the unique hinge-region plasticity of the enzyme without packing bias
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Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: A tool to study the unique hinge-region plasticity of the enzyme without packing bias

机译：低密度的人类蛋白质的水晶包装激酶CK2催化亚基在复杂resorufin或其他配体:一个研究工具独特的铰链区可塑性的酶没有包装的偏见

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摘要

A low-resolution structure of the catalytic subunit CK2 of human protein kinase CK2 (formerly known as casein kinase 2) in complex with the ATP-competitive inhibitor resorufin is presented. The structure supplements previous human CK2 structures in which the interdomain hinge/helix D region adopts a closed conformation correlating to a canonically established catalytic spine as is typical for eukaryotic protein kinases. In the corresponding crystal packing the hinge/helix D region is nearly unaffected by crystal contacts, so that largely unbiased conformational adaptions are possible. This is documented by published human CK2 structures with the same crystal packing but with an open hinge/helix D region, one of which has been redetermined here with a higher symmetry. An overview of all published human CK2 crystal packings serves as the basis for a discussion of the factors that determine whether the open or the closed hinge/helix D conformation is adopted. Lyotropic salts in crystallization support the closed conformation, in which the Phe121 side chain complements the hydrophobic catalytic spine ensemble. Consequently, genuine ligand effects on the hinge/helix D conformation can be best studied under moderate salt conditions. Ligands that stabilize either the open or the closed conformation by hydrogen bonds are known, but a general rule is not yet apparent.
机译：催化的低分辨率的结构亚基CK2的人类蛋白激酶CK2(以前被称为酪蛋白激酶2)在复杂ATP-competitive抑制剂resorufin。补充之前的人类CK2结构结构interdomain铰链/螺旋D采用封闭的构象相关区域正规的确立了催化脊柱是典型的真核蛋白激酶。相应的水晶包装铰链/螺旋D地区几乎是不受晶体联系人,这很大程度上公正的构象适应是有可能的。人类CK2结构相同的晶体包装以开放的铰链/螺旋D地区,但其中一个已经在这里再决定更高的对称性。人类CK2水晶包装作为基础讨论确定的因素是否打开或关闭铰链/螺旋D采用构象。结晶支持封闭的构象,在Phe121侧链的补充疏水催化脊柱。因此,真正的配体的影响铰链/ D螺旋构象可以最好的研究在温和的盐条件下。稳定开放或关闭构象,氢键是已知的,但是一般规则尚不明显。

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