Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins.

@article{Tyukhtenko2008CharacterizationOT,
  title={Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins.},
  author={Sergiy Tyukhtenko and Lalit Deshmukh and Vineet Kumar and Jeffrey W. Lary and James Cole and Vance P. Lemmon and O. B. Vinogradova},
  journal={Biochemistry},
  year={2008},
  volume={47 13},
  pages={4160-8}
}
L1, a highly conserved transmembrane glycoprotein member of the immunoglobulin superfamily of cell adhesion molecules, mediates many developmental processes in the nervous system. Here we present the biophysical characterization and the binding properties of the least structurally defined part of this receptor: its cytoplasmic tail (CT). We have shown by analytical ultracentrifugation and dynamic light scattering experiments that it is mostly monomeric and unstructured in aqueous solution. We… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 39 references

Natively unfolded proteins.

Current opinion in structural biology • 2005
View 7 Excerpts
Highly Influenced

NMR structure determination of proteins and protein complexes larger than 20 kDa.

Current opinion in chemical biology • 1998
View 2 Excerpts
Highly Influenced

Cleavage of L1 in exosomes and apoptotic membrane vesicles released from ovarian carcinoma cells.

Clinical cancer research : an official journal of the American Association for Cancer Research • 2005
View 1 Excerpt

A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins

R Linding
J. Mol. Biol • 2004
View 1 Excerpt

adhesion

J. Qin, O. Vinogradova, E. F. Plow
2004

Similar Papers

Loading similar papers…