title: Identifying protein-protein interactions in somatic hypermutation.
abstract: Somatic hypermutation (SHM) in immunoglobulin genes is required for high affinity antibody-antigen binding. Cultured cell systems, mouse model systems, and human genetic deficiencies have been the key players in identifying likely SHM pathways, whereas "pure" biochemical approaches have been far less prominent, but change appears imminent. Here we comment on how, when, and why biochemistry is likely to emerge from the shadows and into the spotlight to elucidate how the somatic mutation of antibody variable (V) regions is generated.
authors.affiliation: University of Southern California, Los Angeles, CA 90089, USA. mgoodman@usc.edu
authors.forename: Myron F
authors.initials: MF
authors.lastname: Goodman
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Scharff
mesh_terms: D000818:Animals; D004268:DNA-Binding Proteins / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D006801:Humans; D051718:MutS Homolog 2 Protein; D011485:Protein Binding; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D027041:Somatic Hypermutation, Immunoglobulin / Q000235:genetics
chemical_list: D004268:DNA-Binding Proteins; C094443:G-T mismatch-binding protein; D011518:Proto-Oncogene Proteins; D004259:DNA-Directed DNA Polymerase; C497172:MSH2 protein, human; D051718:MutS Homolog 2 Protein