1fsd
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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
1FSD is a Protein complex structure of sequences from Synthetic construct. 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 Sun Nov 18 09:00:27 2007