Unknown

Dataset Information

0

Monobodies as enabling tools for structural and mechanistic biology.


ABSTRACT: Monobodies, built with the scaffold of the fibronectin type III domain, are among the most well-established synthetic binding proteins. They promote crystallization of challenging molecular systems. They have strong tendency to bind to functional sites and thus serve as drug-like molecules that perturb the biological functions of their targets. Monobodies lack disulfide bonds and thus they are particularly suited as genetically encoded reagents to be used intracellularly. This article reviews recent monobody-enabled studies that reveal new structures, molecular mechanisms and potential therapeutic opportunities. A systematic analysis of the crystal structures of monobody-target complexes suggests important attributes that make monobodies effective crystallization chaperones.

SUBMITTER: Hantschel O 

PROVIDER: S-EPMC7370805 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Monobodies as enabling tools for structural and mechanistic biology.

Hantschel Oliver O   Biancalana Matthew M   Koide Shohei S  

Current opinion in structural biology 20200201


Monobodies, built with the scaffold of the fibronectin type III domain, are among the most well-established synthetic binding proteins. They promote crystallization of challenging molecular systems. They have strong tendency to bind to functional sites and thus serve as drug-like molecules that perturb the biological functions of their targets. Monobodies lack disulfide bonds and thus they are particularly suited as genetically encoded reagents to be used intracellularly. This article reviews re  ...[more]

Similar Datasets

| S-EPMC4817051 | biostudies-literature
| S-EPMC6463883 | biostudies-literature
| S-EPMC10292674 | biostudies-literature
| S-EPMC3588166 | biostudies-literature
| S-EPMC7919167 | biostudies-literature
| S-EPMC6318263 | biostudies-literature
| S-EPMC1160177 | biostudies-literature
| S-EPMC3684516 | biostudies-literature
| S-EPMC5098397 | biostudies-literature
| S-EPMC7993322 | biostudies-literature