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Binding and Docking of Synthetic Heterotrimeric Collagen Type IV Peptides with α1β1 Integrin
Author(s) -
Saccà Barbara,
Sinner EvaKathrin,
Kaiser Jens,
Lübken Christoph,
Eble Johannes A.,
Moroder Luis
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020902)3:9<904::aid-cbic904>3.0.co;2-i
Subject(s) - heterotrimeric g protein , integrin , docking (animal) , chemistry , cell adhesion , binding site , collagen receptor , biophysics , stereochemistry , biochemistry , cell , receptor , biology , medicine , nursing , g protein
Checking the register : Cell‐adhesion processes are mediated by conformation‐dependent binding of collagen type IV to integrins. Two heterotrimeric collagen peptides that contain the residue‐457–468 sequence of the cell‐adhesion epitope of the α1 and α2 chains in collagen type IV were synthesized and the three chains were assembled into the α1α2α1′ and α2α1α1′ registers (see figure). Binding and modeling experiments allowed identification of the latter register as the most plausible alignment of the chains in natural collagen type IV.