Linked Life Data

21203951

Source:http://linkedlifedata.com/resource/pubmed/id/21203951

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-1-4
pubmed:abstractText
We here present a detailed study of the ligand-receptor interactions between single and triple-helical strands of collagen and the ?2A domain of integrin (?2A), providing valuable new insights into the mechanisms and dynamics of collagen-integrin binding at a sub-molecular level. The occurrence of single and triple-helical strands of the collagen fragments was scrutinized with atom force microscopy (AFM) techniques. Strong interactions of the triple-stranded fragments comparable to those of collagen can only be detected for the 42mer triple-helical collagen-like peptide under study (which contains 42 amino acid residues per strand) by solid phase assays as well as by surface plasmon resonance (SPR) measurements. However, changes in NMR signals during titration and characteristic saturation transfer difference (STD) NMR signals are also detectable when ?2A is added to a solution of the 21mer single-stranded collagen fragment. Molecular dynamics (MD) simulations employing different sets of force field parameters were applied to study the interaction between triple-helical or single-stranded collagen fragments with ?2A. It is remarkable that even single-stranded collagen fragments can form various complexes with ?2A showing significant differences in the complex stability with identical ligands. The results of MD simulations are in agreement with the signal alterations in our NMR experiments, which are indicative of the formation of weak complexes between single-stranded collagen and ?2A in solution. These results provide useful information concerning possible interactions of ?2A with small collagen fragments that are of relevance to the design of novel therapeutic A-domain inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1674-8018
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
393-405
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Interaction of the ?2A domain of integrin with small collagen fragments.
pubmed:affiliation
Institut für Biochemie und Endokrinologie, Veterinärmedizinische Fakultät, Justus-Liebig-Universität Gießen, Frankfurter Str. 100, 35392 Gießen, Germany. Hans-Christian.Siebert@vetmed.uni-giessen.de
pubmed:publicationType
Journal Article, Comparative Study