Alternate protein frameworks for molecular recognition.
Proc Natl Acad Sci U S A
; 92(14): 6552-6, 1995 Jul 03.
Article
em En
| MEDLINE
| ID: mdl-7604031
ABSTRACT
In an effort to determine whether proteins with structures other than the immunoglobulin fold can be used to mimic the ligand binding properties of antibodies, we generated a library from the four-helix bundle protein cytochrome b562 in which the two loops were randomized. Panning of this library against the bovine serum albumin (BSA) conjugate of N-methyl-p-nitrobenzylamine derivative 1 by phage display methods yielded cytochromes in which residues Trp-20, Arg-21, and Ser-22 in loop A and Arg-83 and Trp-84 in loop B were conserved. The individual mutants, which fold into native-like structure, bind selectively to the BSA-1 conjugate with micromolar dissociation constants (Kd), in comparison to a monoclonal antibody that binds selectively to 1 with a Kd of 290 nM. These and other antibody-like receptors may prove useful as therapeutic agents or as reagents for both intra- and extracellular studies.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Estrutura Secundária de Proteína
/
Grupo dos Citocromos b
/
Proteínas de Escherichia coli
Tipo de estudo:
Clinical_trials
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Estados Unidos