Publication Abstract from PubMed
Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.
Structures of two repeats of spectrin suggest models of flexibility.,Grum VL, Li D, MacDonald RI, Mondragon A Cell. 1999 Aug 20;98(4):523-35. PMID:10481916[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
