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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding
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Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding

机译：基因定点突变体的结构分析细胞视黄结合蛋白II地址结构之间的关系完整性和配体结合

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摘要

The structural integrity of cellular retinoic acid-binding protein II (CRABPII) has been investigated using the crystal structures of CRABPII mutants. The overall fold was well maintained by these CRABPII mutants, each of which carried multiple different mutations. A water-mediated network is found to be present across the large binding cavity, extending from Arg111 deep inside the cavity to the α2 helix at its entrance. This chain of interactions acts as a 'pillar' that maintains the integrity of the protein. The disruption of the water network upon loss of Arg111 leads to decreased structural integrity of the protein. A water-mediated network can be re-established by introducing the hydrophilic Glu121 inside the cavity, which results in a rigid protein with the α2 helix adopting an altered conformation compared with wild-type CRABPII.
机译：细胞视黄的结构完整性结合蛋白II (CRABPII)调查使用的晶体结构CRABPII突变体。由这些CRABPII突变体,每个进行多个不同的突变。water-mediated网络发现在绑定腔大,扩展Arg111腔深处的α2螺旋它的入口。一个“支柱”,维护的完整性蛋白质。Arg111导致结构性下降的损失完整的蛋白质。网络可以重新引入亲水Glu121腔内,结果在一个刚性的蛋白质的α2螺旋采用一个构象而改变野生型CRABPII。

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