Functional proteins designed de novo have potential application in chemical engineering, agriculture and healthcare. Metal binding sites are commonly used to incorporate functions. Based on a de novo designed protein DS119 with a beta alpha beta structure, we have computationally engineered zinc binding sites into it using a home-made searching program. Seven out of the eight designed sequences tested were shown to bind Zn2+ with micromolar affinity, and one of them bound Zn2+ with 1:1 stoichiometry. This is the first time that metalloproteins with an alpha, beta mixed structure have been designed from scratch.Cell BiologySCI(E)PubMed中国科学引文数据库(CSCD)6ARTICLE121006-1013
ABSTRACT: Genetically encoded unnatural amino acids could facilitate the design of proteins and enzy...
International audienceHydrolytic zinc enzymes are common targets for protein design. The versatility...
Proteins can make use of metal ions to bind substrates, to maintain structure, to effect catalysis...
Approximately one third of proteins are thought to bind metal ions. These ions often improve the pro...
Creating proteins with new functions is a challenging task in the field of protein design. While var...
Engineered proteins will continue to expand the molecular toolkit for applications in medicine, biot...
Structure-based protein design tests our understanding of the minimal determinants of protein struct...
The structures and reactions of metal ions in proteins are of tremendous interest in bioinorganic ch...
The de novo design of functional proteins requires specification of tertiary structure and incorpora...
Selective metal binding is a key requirement not only for the functions of natural metalloproteins b...
Metalloenzymes catalyze a wide variety of reactions in nature by taking advantage of the versatility...
Metal binding proteins or metalloproteins chelate a metal ion cofactor such as iron, zinc, or copper...
ABSTRACT: A semi-automated, rational design strategy has been used to introduce a family of seven si...
AbstractThe recently determined structure of a zinc binding peptide reveals that a particular sequen...
BackgroundSpecific interactions of metal ions with proteins are central to all life processes. The v...
ABSTRACT: Genetically encoded unnatural amino acids could facilitate the design of proteins and enzy...
International audienceHydrolytic zinc enzymes are common targets for protein design. The versatility...
Proteins can make use of metal ions to bind substrates, to maintain structure, to effect catalysis...
Approximately one third of proteins are thought to bind metal ions. These ions often improve the pro...
Creating proteins with new functions is a challenging task in the field of protein design. While var...
Engineered proteins will continue to expand the molecular toolkit for applications in medicine, biot...
Structure-based protein design tests our understanding of the minimal determinants of protein struct...
The structures and reactions of metal ions in proteins are of tremendous interest in bioinorganic ch...
The de novo design of functional proteins requires specification of tertiary structure and incorpora...
Selective metal binding is a key requirement not only for the functions of natural metalloproteins b...
Metalloenzymes catalyze a wide variety of reactions in nature by taking advantage of the versatility...
Metal binding proteins or metalloproteins chelate a metal ion cofactor such as iron, zinc, or copper...
ABSTRACT: A semi-automated, rational design strategy has been used to introduce a family of seven si...
AbstractThe recently determined structure of a zinc binding peptide reveals that a particular sequen...
BackgroundSpecific interactions of metal ions with proteins are central to all life processes. The v...
ABSTRACT: Genetically encoded unnatural amino acids could facilitate the design of proteins and enzy...
International audienceHydrolytic zinc enzymes are common targets for protein design. The versatility...
Proteins can make use of metal ions to bind substrates, to maintain structure, to effect catalysis...