Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1984-9-18
pubmed:abstractText
The tertiary structures of thioredoxin from Escherichia coli and bacteriophage T4 have been compared and aligned giving a common fold of 68 C alpha atoms with a root mean square difference of 2.6 A. The amino acid sequence of glutaredoxin has been aligned to those of the thioredoxins assuming that glutaredoxin has the same common fold. A model of the glutaredoxin molecule was built on a vector display using this alignment and the T4 thioredoxin tertiary structure. By comparison of the model with those of the thioredoxins, we have identified a molecular surface area on one side of the redox-active S-S bridge which we suggest is the binding area of these molecules for redox interactions with other proteins. This area comprises residues 33-34, 75-76 and 91-93 in E. coli thioredoxin; 15-16, 65-66 and 76-78 in T4 thioredoxin and 12-13, 59-60 and 69-71 in glutaredoxin. In all three molecules, this part of the surface is flat and hydrophobic. Charged groups are completely absent. In contrast, there is a cluster of charged groups on the other side of the S-S bridge which we suggest participates in the mechanisms of the redox reactions. In particular, a lysine residue close to an aromatic ring is conserved in all molecules.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-1094461, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-12009, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-235528, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-359548, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-366603, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-372193, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-382982, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-385588, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-39074, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-391270, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-412850, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4152559, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4374553, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4382243, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4390809, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4552684, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4565673, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4883076, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-4945270, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-537063, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-6351859, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-6352262, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-7009607, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-7021558, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-768986, http://linkedlifedata.com/resource/pubmed/commentcorrection/6378624-7783
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1443-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Conformational and functional similarities between glutaredoxin and thioredoxins.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't