A Zinc-binding Domain Involved in the Dimerization of RAG1
Rodgers K, Bu Z, Fleming K, Schatz D, Engelman D, Coleman J. A Zinc-binding Domain Involved in the Dimerization of RAG1. Journal Of Molecular Biology 1996, 260: 70-84. PMID: 8676393, DOI: 10.1006/jmbi.1996.0382.Peer-Reviewed Original ResearchConceptsRecombination-activating gene 1Zinc-binding motifDimerization domainZinc fingerProtein-protein interactionsLymphoid-specific genesN-terminal thirdZinc finger sequencesAmino acid residuesC3HC4 motifRAG1 sequencesRAG1 proteinTerminal domainHomodimer formationAcid residuesBiophysical techniquesGene 1Energetics of associationMonomeric subunitsMotifProteinFinger sequencesSequenceC3HC4Zinc ionsrag-1 and rag-2: Biochemistry and Protein Interactions
Schatz D, Leu T. rag-1 and rag-2: Biochemistry and Protein Interactions. Current Topics In Microbiology And Immunology 1996, 217: 11-29. PMID: 8787615, DOI: 10.1007/978-3-642-50140-1_2.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsRAG-1Protein-protein interactionsRAG-2 proteinT-cell receptor proteinsSite-specific recombination reactionLymphocyte-specific factorsProtein interactionsEnzymatic machineryGene productsRAG-2Lymphocyte developmentReceptor proteinBiochemical propertiesProteinCoordinated activityGenesTerminal deoxynucleotidyl transferaseRecombinationDiversityDeoxynucleotidyl transferaseMost componentsMachineryNucleotidesSpeciesTransferase