Linked Life Data

3754866

Source:http://linkedlifedata.com/resource/pubmed/id/3754866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1986-7-2
pubmed:abstractText
We have combined amino acid sequence data with x-ray diffraction results to determine differences in structure of wheat germ agglutinin isolectin 1 (WGA1) relative to the known structure of wheat germ agglutinin isolectin 2 (WGA2). Electron density difference maps computed at 2.2 A resolution with coefficients [2F(WGA1) - F(WGA2)] and [F(WGA1) - F(WGA2)] and based on refined model phases of the WGA2 structure have revealed that the largest differences in the two isolectin structures are localized in the B-domain of the molecule. Amino acid sequence studies of tryptic and thermolytic peptides of WGA1 confirm the strong homology between the two isolectins and suggest variability at only four sequence positions. Three of these are closely spaced in domain B. The two histidines in WGA2, His59 and His66, are substituted by Gln and Tyr, respectively, and Pro56, by Thr in WGA1. The fourth difference at position 93 in domain C was identified as a change from Ser (WGA2) to Ala (WGA1). With these substitutions WGA1 exhibits a slightly higher degree of internal homology than does WGA2. In addition, we have carried out fluorescence studies on tryptic peptide T-3 to confirm the presence of a second Trp residue in the wheat germ agglutinin molecule, recently predicted at position 41 during the course of high resolution crystal structure refinement of WGA2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7191-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Structural differences in the two major wheat germ agglutinin isolectins.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.