Camelid nanobodies: killing two birds with one stone. (June 2015)

• Record Type: Journal Article
• Authors: Desmyter, Aline; Spinelli, Silvia; Roussel, Alain; Cambillau, Christian
• Is Part Of: Current opinion in structural biology. Volume 32(2015)
• Page Start: 1
• Page End: 8
• Publication Date: 2015-06
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2015.01.001
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: Camelid nanobodies (or VHHs) facilitate proteins crystallization. They preferentially bind concave surfaces such as protein active sites or hinges. They are easily produced in Escherichia coli . Abstract : In recent years, the use of single-domain camelid immunoglobulins, termed vHHs or nanobodies, has seen increasing growth in biotechnology, pharmaceutical applications and structure/function research. The usefulness of nanobodies in structural biology is now firmly established, as they provide access to new epitopes in concave and hinge regions — and stabilize them. These sites are often associated with enzyme inhibition or receptor neutralization, and, at the same time, provide favorable surfaces for crystal packing. Remarkable results have been achieved by using nanobodies with flexible multi-domain proteins, large complexes and, last but not least, membrane proteins. While generating nanobodies is still a rather long and expensive procedure, the advent of naive libraries might be expected to facilitate the whole process.