STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING
STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING
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DOI：
10.1126/science.1721241
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发表时间：
1991-12-13
期刊：
影响因子：
56.9
通讯作者：
HENDRICKSON, WA
中科院分区：
文献类型：
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作者：
WEIS, WI;KAHN, R;HENDRICKSON, WA
钙依赖性（C型）动物凝集素参与许多由蛋白质-碳水化合物相互作用介导的细胞表面识别事件。C型凝集素家族包括细胞粘附分子、内吞受体和细胞外基质蛋白。哺乳动物甘露糖结合蛋白是一种C型凝集素，其功能是不依赖抗体的宿主防御病原体。的碳水化合物识别结构域的大鼠甘露糖结合蛋白，确定为钬取代的复合物的多波长异常色散（MAD）相位的晶体结构，揭示了一个不寻常的折叠组成的两个不同的区域，其中之一包含广泛的不规则的二级结构稳定的两个钬离子。该结构解释了所有C型碳水化合物识别结构域中32个残基的保守性，这表明这里看到的折叠是这些结构域共有的。在Ho L（III）边缘观察到的强异常散射表明，传统的重原子络合物一般都适用于MAD定相方法。
Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho L(III) edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.