Linked Life Data

9030762

Source:http://linkedlifedata.com/resource/pubmed/id/9030762

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1997-3-20
pubmed:abstractText
NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydonmonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 phi dihedral restraints. The structure of C. reinhardtii thioredoxin h was solved in its oxidised form, and the ensemble of 23 converged structures superpose to the geometric average structure with an atomic rmsd of 0.080 nm +/- 0.016 for the (N, C(alpha), C) backbone atoms of residues 4-110. Comparisons with other thioredoxins, such as thioredoxin from the bacterium Escherichia coli, thioredoxin 2 from a cyanobacterium of the Anabaena genus, and human thioredoxin, showed that thioredoxin h models share more structural features with human thioredoxin than with other bacterial thioredoxins. Examination of the accessible surface around the redoxactive peptide sequence indicates that a potent thioredoxin-h-substrate interaction could be similar to the vertebrate thioredoxin-substrate interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
374-83
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii.
pubmed:affiliation
Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't