Journal article

The use of coiled-coil interactions for the analysis and micropreparative isolation of adenomatous polyposis coli protein complexes

J Wade, L Otvos, A Burgess, E Nice, J Rothacker, M Nerrie, M Faux, B Catimel

Journal of Peptide Research | BLACKWELL MUNKSGAARD | Published : 2001

Abstract

The coiled coil is a common structural motif found both as the dominant structure in fibrous proteins and as an oligomerization domain in a variety of cytoskeletal and extracellular matrix proteins. Coiled-coils typically consist of two to four helices that are supercoiled around one another in either parallel or antiparallel orientations. In the past few years our knowledge of the structure and specificity of coiled coil interactions has increased, allowing the de novo design and preparation of coiled-coils with well-defined structure and specificity. Indeed, the design and synthesis of a peptide that binds specifically to a single coiled-coil-containing protein, adenomatous polyposis coli ..

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University of Melbourne Researchers