Linked Life Data

19738200

Source:http://linkedlifedata.com/resource/pubmed/id/19738200

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
87
pubmed:dateCreated
2009-9-9
pubmed:abstractText
Multicellular organisms rely on complex, fine-tuned protein networks to respond to environmental changes. We used in vitro evolution to explore the role of domain mutation and expansion in the evolution of network complexity. Using random mutagenesis to facilitate family expansion, we asked how versatile and robust the binding site must be to produce the rich functional diversity of the natural PDZ domain family. From a combinatorial protein library, we analyzed several hundred structured domain variants and found that one-quarter were functional for carboxyl-terminal ligand recognition and that our variant repertoire was as specific and diverse as the natural family. Our results show that ligand binding is hardwired in the PDZ fold and suggest that this flexibility may facilitate the rapid evolution of complex protein interaction networks.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1937-9145
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
ra50
pubmed:dateRevised
2010-9-21
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Rapid evolution of functional complexity in a domain family.
pubmed:affiliation
Department of Protein Engineering, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.
pubmed:publicationType
Journal Article