Structural highlights
Publication Abstract from PubMed
A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion.
A novel ADP- and zinc-binding fold from function-directed in vitro evolution.,Lo Surdo P, Walsh MA, Sollazzo M Nat Struct Mol Biol. 2004 Apr;11(4):382-3. Epub 2004 Mar 14. PMID:15024384[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lo Surdo P, Walsh MA, Sollazzo M. A novel ADP- and zinc-binding fold from function-directed in vitro evolution. Nat Struct Mol Biol. 2004 Apr;11(4):382-3. Epub 2004 Mar 14. PMID:15024384 doi:10.1038/nsmb745
