Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex
Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex
复制标题
DOI：
10.1016/s1097-2765(00)80406-2
复制
发表时间：
2000-01-01
期刊：
影响因子：
16
通讯作者：
Schatz, DG
中科院分区：
文献类型：
--
作者：
Fugmann, SD;Villey, IJ;Schatz, DG
在V（D）J重组过程中，RAG 1和RAG 2蛋白协同催化一系列DNA键断裂和链转移反应。RAG介导的催化作用所涉及的活性位点的结构、位置和数量尚未确定。使用蛋白质二级结构预测算法，我们已经确定了一个区域的RAG 1与转座酶和逆转录病毒整合酶的活性位点区域的可能的结构相似性。基于这些信息，我们已经确定了RAG 1（D 600和D 708）中的两个天冬氨酸残基，其在催化中具有特异性功能。结果支持一个模型，其中RAG 1包含一个单一的，二价金属离子结合活性位点结构相关的转座酶/整合酶的活性位点，并负责所有的催化功能的RAG蛋白复合物。
During V(D)J recombination, the RAG1 and RAG2 proteins cooperate to catalyze a series of DNA bond breakage and strand transfer reactions. The structure, location, and number of active sites involved in RAG-mediated catalysis have as yet not been determined. Using protein secondary structure prediction algorithms, we have identified a region of RAG1 with possible structural similarities to the active site regions of transposases and retroviral integrases. Based on this information, we have identified two aspartic acid residues in RAG1 (D600 and D708) that function specifically in catalysis. The results support a model in which RAG1 contains a single, divalent metal ion binding active site structurally related to the active sites of transposases/integrases and responsible for all catalytic functions of the RAG protein complex.