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Curr Opin Struct Biol. 2015 Jun;32:1-8. doi: 10.1016/j.sbi.2015.01.001. Epub 2015 Jan 19.

Camelid nanobodies: killing two birds with one stone.

Author information

1
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, France; Centre National de la Recherche Scientifique, AFMB, UMR 7257, case 932, 13288 Marseille Cedex 09, France.
2
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, France; Centre National de la Recherche Scientifique, AFMB, UMR 7257, case 932, 13288 Marseille Cedex 09, France. Electronic address: cambillau@afmb.univ-mrs.fr.

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.

PMID:
25614146
DOI:
10.1016/j.sbi.2015.01.001
[Indexed for MEDLINE]

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