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

Saccà, B.; Sinner, E.-K.; Kaiser, J.; Lübken, C.; Eble, J. A.; Moroder, L.

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

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

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

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

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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: https://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.