Conversion of monomeric protein L to an obligate dimer by computational protein design
AUTOR(ES)
Kuhlman, Brian
FONTE
The National Academy of Sciences
RESUMO
Protein L consists of a single α-helix packed on a four-stranded β-sheet formed by two symmetrically opposed β-hairpins. We use a computer-based protein design procedure to stabilize a domain-swapped dimer of protein L in which the second β-turn straightens and the C-terminal strand inserts into the β-sheet of the partner. The designed obligate dimer contains three mutations (A52V, N53P, and G55A) and has a dissociation constant of ≈700 pM, which is comparable to the dissociation constant of many naturally occurring protein dimers. The structure of the dimer has been determined by x-ray crystallography and is close to the in silico model.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=58527Documentos Relacionados
- Conversion of a maltose receptor into a zinc biosensor by computational design
- Specificity versus stability in computational protein design
- Enzyme-like proteins by computational design
- The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors
- Bonded Joints Design Aided by Computational Tool