Linked Life Data

11025548

Source:http://linkedlifedata.com/resource/pubmed/id/11025548

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-12-20
pubmed:abstractText
Actin-depolymerizing factor (ADF) and cofilin define a family of actin-binding proteins essential for the rapid turnover of filamentous actin in vivo. Here we present the 2.0 A crystal structure of Arabidopsis thaliana ADF1 (AtADF1), the first plant crystal structure from the ADF/cofilin (AC) family. Superposition of the four AC isoform structures permits an accurate sequence alignment that differs from previously reported data for the location of vertebrate-specific inserts and reveals a contiguous, vertebrate-specific surface opposite the putative actin-binding surface. Extending the structure-based sequence alignment to include 30 additional isoforms indicates three major groups: vertebrates, plants, and "other eukaryotes." Within these groups, several structurally conserved residues that are not conserved throughout the entire AC family have been identified. Residues that are highly conserved among all isoforms tend to cluster around the tryptophan at position 90 and a structurally conserved kink in alpha-helix 3. Analysis of surface character shows the presence of a hydrophobic patch and a highly conserved acidic cluster, both of which include several residues previously implicated in actin binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
374-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11025548-Actin Depolymerizing Factors, pubmed-meshheading:11025548-Amino Acid Sequence, pubmed-meshheading:11025548-Animals, pubmed-meshheading:11025548-Arabidopsis, pubmed-meshheading:11025548-Conserved Sequence, pubmed-meshheading:11025548-Crystallography, pubmed-meshheading:11025548-DNA Transposable Elements, pubmed-meshheading:11025548-Destrin, pubmed-meshheading:11025548-Hydrogen-Ion Concentration, pubmed-meshheading:11025548-Microfilament Proteins, pubmed-meshheading:11025548-Models, Molecular, pubmed-meshheading:11025548-Molecular Sequence Data, pubmed-meshheading:11025548-Multigene Family, pubmed-meshheading:11025548-Plant Proteins, pubmed-meshheading:11025548-Sequence Homology, Amino Acid, pubmed-meshheading:11025548-Surface Properties, pubmed-meshheading:11025548-Vertebrates
pubmed:year
2000
pubmed:articleTitle
A comparative structural analysis of the ADF/cofilin family.
pubmed:affiliation
Department of Molecular Biology, Lewis Thomas Laboratories, Princeton University, Princeton, New Jersey 08544, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't