ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY
ANALOGOUS INHIBITORS OF ELASTASE DO NOT ALWAYS BIND ANALOGOUSLY
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DOI：
10.1038/nsb0194-55
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发表时间：
1994-01-01
期刊：
影响因子：
--
通讯作者：
RINGE, D
中科院分区：
文献类型：
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作者：
MATTOS, C;RASMUSSEN, B;RINGE, D
已经假设单个抑制剂复合物的结构足以定义具有独特结合位点和独特定义的配体结合模式的酶的可用亚位点-因此可以通过动力学实验探测这些亚位点的特异性。弹性蛋白酶是一种酶，这些传统的假设，这些结构和动力学研究的基础，不成立。三个新的弹性蛋白酶的晶体结构复杂的化学相似的抑制剂具有相似的结合亲和力揭示了结合模式的多样性，以及两个新的弹性蛋白酶的亚位点。这种类似抑制剂的多个结合位点和不同结合模式的存在表明，研究人员在使用动力学绘制蛋白质亚位点时必须谨慎进行。
It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding - the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites.