| Literature DB >> 15024384 |
Paola Lo Surdo1, Martin A Walsh, Maurizio Sollazzo.
Abstract
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.Entities:
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Year: 2004 PMID： 15024384 DOI： 10.1038/nsmb745
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369