Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937086 | Biochemical and Biophysical Research Communications | 2007 | 5 Pages |
Abstract
The third domain of the low-density lipoprotein receptor-associated protein (RAP d3) binds with high-affinity to pairs of complement-type repeats (CR) within the LDLR family of receptors. Structural analyses have defined the contact surface between RAP d3 and a CR pair from the low-density lipoprotein receptor (LDLR). Much of the sequence of RAP d3 has been proposed to stabilize the receptor-binding region without participating directly in formation of the contact surface. We have developed a truncated version of RAP d3 in which these scaffolding regions are excised and replaced with a single, intramolecular disulfide bond. This substitution allows for deletion of as much as a third of the RAP d3 sequence with substantial retention of receptor-binding ability.
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Authors
Sara L. Isbell, Simone B. Haslam, Todd C. Zankel,