A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity.

@article{Breustedt2009ANC,
  title={A new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavity.},
  author={Daniel A Breustedt and Lorenz Chatwell and Arne Skerra},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2009},
  volume={65 Pt 10},
  pages={1118-25}
}
Tear lipocalin (TLC) with the bound artificial ligand 1,4-butanediol has been crystallized in space group P2(1) with four protein molecules in the asymmetric unit and its X-ray structure has been solved at 2.6 A resolution. TLC is a member of the lipocalin family that binds ligands with diverse chemical structures, such as fatty acids, phospholipids and cholesterol as well as microbial siderophores and the antibiotic rifampin. Previous X-ray structural analysis of apo TLC crystallized in space… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-6 of 6 references

Lipocalins. Georgetown: Landes Bioscience

  • B. Åkerström, N. Borregaard, D. A. Flower, Salier, J.-S
  • 2006
2 Excerpts

The PyMOL Molecular Graphics System

  • W. L. DeLano
  • DeLano Scientific LLC, San Carlos, California…
  • 2002
2 Excerpts

Biochemistry, 39, 1935–1941

  • R. K. Strong
  • Israili, Z. H. & Dayton, P. G. (2001). Drug Metab…
  • 2000

Biochim

  • D. R. Flower
  • Biophys. Acta, 1482, 46–56.
  • 2000

Biochem

  • D. R. Flower
  • J. 318, 1–14.
  • 1996
2 Excerpts

Curr

  • W. L. Hubbell
  • Eye Res. 14, 363–372. Goetz, D. H., Willie, S. T…
  • 1995

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