Article ID Journal Published Year Pages File Type
10764371 Biochemical and Biophysical Research Communications 2010 7 Pages PDF
Abstract
► IGFBP-5 structures containing N, L, and C domains were separately modeled. ► The L domain of IGFBP-5 was expressed in Escherichia coli and purified. ► The L domain structure of IGFBP-5 was similar to that of the corepressor of repressor element-1 silencing transcription factor (CoREST) linker. ► The purified L domain existed as a homogenous dimer in glutaraldehyde crosslinking.
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