Linked Life Data

3273222

Source:http://linkedlifedata.com/resource/pubmed/id/3273222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-5-9
pubmed:abstractText
The solution conformation of the second loop fragment of human EGF, [Ala20] EGF (14-31), was determined using two-dimensional NMR homonuclear Hartmann-Hahn and rotating frame nuclear Overhauser enhancement spectroscopy. The results are compared with the conformation of the second loop fragment of human TGF-alpha, [Ala21] TGF-alpha(16-32), and with that of the second loop of intact EGF. Comparison of the two experimentally determined structures of the second loop fragments shows significant differences in the turn regions of each peptide. For the EGF fragment, hydrophobic side chain groups protrude away from the ring, whereas for the TGF-alpha fragment hydrophilic groups are directed away from the ring. Although these turn regions represent the putative receptor binding sites, neither second loop fragment binds to the EGF receptor. The biological activity is discussed in terms of the conformational differences found for the two second loop fragments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0952-3499
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
116-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Conformational and receptor binding properties of human EGF and TGF-alpha second loop fragments.
pubmed:affiliation
Laboratory of Chemistry, NHLBI, National Institutes of Health, Bethesda, MD 20892.
pubmed:publicationType
Journal Article