1fsd
FULL SEQUENCE DESIGN 1 (FSD-1) OF BETA BETA ALPHA MOTIF, NMR, 41 STRUCTURES
OverviewOverview
The first fully automated design and experimental validation of a novel sequence for an entire protein is described. A computational design algorithm based on physical chemical potential functions and stereochemical constraints was used to screen a combinatorial library of 1.9 x 10(27) possible amino acid sequences for compatibility with the design target, a betabetaalpha protein motif based on the polypeptide backbone structure of a zinc finger domain. A BLAST search shows that the designed sequence, full sequence design 1 (FSD-1), has very low identity to any known protein sequence. The solution structure of FSD-1 was solved by nuclear magnetic resonance spectroscopy and indicates that FSD-1 forms a compact well-ordered structure, which is in excellent agreement with the design target structure. This result demonstrates that computational methods can perform the immense combinatorial search required for protein design, and it suggests that an unbiased and quantitative algorithm can be used in various structural contexts.
About this StructureAbout this Structure
The following page contains interesting information on the relation of 1FSD with [Designer Proteins]. Full crystallographic information is available from OCA.
ReferenceReference
De novo protein design: fully automated sequence selection., Dahiyat BI, Mayo SL, Science. 1997 Oct 3;278(5335):82-7. PMID:9311930 Page seeded by OCA on Fri May 2 16:42:40 2008