Published online 14 February 2005 doi:10.1084/jem.20050161
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 201, Number 4, 493-496
Identifying proteinprotein interactions in somatic hypermutation
Myron F. Goodmana,b and
Matthew D. Scharffa,b
a M.F.G. is at University of Southern California, Los Angeles, CA 90089.
b M.D.S. is at Albert Einstein College of Medicine, Bronx, NY 10461.
CORRESPONDENCE M.F.G.: mgoodman{at}usc.edu
Abstract
Somatic hypermutation (SHM) in immunoglobulin genes is required for high affinity antibodyantigen 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.

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