User:Tgwgraham1/sandbox

Structure
Rad50 is a member of the structural maintenance of chromosomes (SMC) family of proteins.

Rad50 is a member of the structural maintenance of chromosomes (SMC) family of proteins. Like other SMC proteins, Rad50 contains a long internal coiled-coil domain that folds back on itself, bringing the N- and C-termini together to form a globular ABC ATPase head domain. Rad50 can dimerize both through its head domain and through a zinc-binding dimerization motif at the opposite end of the coiled-coil known as the “zinc-hook”. Results from atomic force microscopy suggest that in free Mre11-Rad50-Nbs1 complexes, the zinc-hooks of a single Rad50 dimer associate to form a closed loop. Upon binding to a DNA end, however, the zinc-hooks appear to snap apart, adopting a conformation that is thought to enable zinc-hook-mediated tethering of broken ends.

tgwgraham (talk) 18:13, 2 July 2012 (UTC)