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Structural Studies on the Ca~(2+)-binding Domain of Human Nucleobindin (Calnuc)

机译：人核结合素（Calnuc）Ca〜（2+）结合域的结构研究

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摘要

Nucleobindin,also known as calnuc,participates in Ca~(2+) storage in the Golgi,as well as in other biological processes that involve DNA-binding and protein-protein interactions.We have determined the three-dimensional solution structure of the Ca~(2+)-binding domain of nucleobindin by NMR showing that it consists of two EF-hand motifs.The NMR structure indicates that the phi and psi angles of residues in both motifs are very similar,despite the noncanonical sequence of the C-terminal EF-hand,which contains an arginine residue instead of the typical glycine at the sixth position of the 12-residue loop.The relative orientation of the a-helices in the N-terminal EF-hand falls within the common arrangement found in most EF-hand structures.In contrast,the noncanonical EF-hand deviates from the average orientation.The two helix-loop-helix moieties are in the open conformation characteristic of the Ca~(2+)-bound state.We find that both motifs bind Ca~(2+) with apparent dissociation constants of 47 and 40 muM for the noncanonical and the canonical EF-hand,respectively.The Ca~(2+)-binding domain of nucleobindin is unstructured in the absence of Ca~(2+) and folds upon Ca~(2+) addition.NMR relaxation data and structural studies of the folded domain indicate that it undergoes slow dynamics,suggesting that it is floppier and less compact than a globular domain.
机译：核结合素，也称为钙蛋白，参与高尔基体中Ca〜（2+）的储存以及参与涉及DNA结合和蛋白质-蛋白质相互作用的其他生物过程。我们确定了Ca的三维溶液结构核苷的〜（2 +）-结合结构域通过NMR显示它由两个EF-手基序组成.NMR结构表明，尽管C-的非规范序列，两个基序中残基的phi和psi角非常相似。末端EF-hand，它在12残基环的第六位含有一个精氨酸残基而不是典型的甘氨酸.N末端EF-hand中a螺旋的相对方向属于大多数情况下的常见排列EF-手结构。相反，非经典EF-手偏离平均方向。两个螺旋-环-螺旋部分处于Ca〜（2+）结合状态的开放构象特征。我们发现两个基序以明显的离解常数结合Ca〜（2+）分别为非常规和常规EF-手的47和40μM。核键蛋白的Ca〜（2+）结合结构域在没有Ca〜（2+）的情况下是无结构的并且在Ca〜（2+）上折叠NMR弛豫数据和折叠结构域的结构研究表明，它经历了缓慢的动力学过程，这表明它比球状结构域更蓬松且紧凑。

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