Linked Life Data

3255102

Source:http://linkedlifedata.com/resource/pubmed/id/3255102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-9-21
pubmed:abstractText
The model structure previously proposed for human C5a, based upon the crystal structure of the homologous protein human C3a, is compared to the solution structure of human C5a recently determined by nuclear magnetic resonance (NMR) methods in our laboratory. The general folding and helix topography of the C5a protein were modeled very well. The N-terminus, which is disordered in the C3a crystal, was correctly predicted in the C5a model both as to its being a helix and as to its docking site on the rest of the molecule. On the other hand, the NMR data show that the biologically important C-terminal residues are disordered in solution, unlike the model and the C3a crystal structure where this region was helical.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Comparison of model and nuclear magnetic resonance structures for the human inflammatory protein C5a.
pubmed:affiliation
NMR Research Group, Abbott Laboratories, Abbott Park, Illinois 60064.
pubmed:publicationType
Journal Article, Comparative Study