de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Binding and docking of synthetic heterotrimeric collagen type IV peptides with alpha1 beta1 integrin

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78593

Saccà,  B.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78715

Sinner,  E.-K.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78419

Moroder,  L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Saccà, B., Sinner, E.-K., Kaiser, J., Lübken, C., Eble, J. A., & Moroder, L. (2002). Binding and docking of synthetic heterotrimeric collagen type IV peptides with alpha1 beta1 integrin. ChemBioChem, 3(9), 904-907.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6E5E-D
Abstract
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 alpha1 and alpha2 chains in collagen type IV were synthesized and the three chains were assembled into the alpha1alpha2alpha1' and alpha2alpha1alpha1' 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.