换一批Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection.
第一作者：
Joseph J,Maciag
第一单位：
Department of Biology, University of Texas at Arlington, Arlington, TX 76019; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695.
作者：
医学主题词
别构调节(Allosteric Regulation);别构部位(Allosteric Site);氨基酸取代(Amino Acid Substitution);半胱氨酸天冬氨酸蛋白酶3(Caspase 3);催化域(Catalytic Domain);结晶学, X线(Crystallography, X-Ray);酶激活(Enzyme Activation);模型, 分子(Models, Molecular);分子构象(Molecular Conformation);分子动力学模拟(Molecular Dynamics Simulation);诱变(Mutagenesis);蛋白质结合(Protein Binding);蛋白质构象(Protein Conformation);蛋白质多聚化(Protein Multimerization);量化构效关系(Quantitative Structure-Activity Relationship);溶解度(Solubility);水(Water)
DOI
10.1073/pnas.1603549113
PMID
27681633
发布时间
2018-11-13
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