Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.

@article{Konrat1998StructureOC,
  title={Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.},
  author={Robert Konrat and Bernhard Kr{\"a}utler and Ralf Weiskirchen and Klaus Bister},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 36},
  pages={23233-40}
}
Members of the cysteine- and glycine-rich protein family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control, and pathogenesis. Here we report the solution structure of full-length recombinant quail CRP2 as determined by multi-dimensional triple-resonance NMR spectroscopy. The structural analysis revealed that the global fold of the two LIM… CONTINUE READING
Highly Cited
This paper has 152 citations. REVIEW CITATIONS
12 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

152 Citations

0204060'97'02'08'14
Citations per Year
Semantic Scholar estimates that this publication has 152 citations based on the available data.

See our FAQ for additional information.

References

Publications referenced by this paper.

Structure and Dynamics

  • R. Koradi, M. Billeter, K. Wüthrich
  • J. Mol. Graphics 14,
  • 1996

Similar Papers

Loading similar papers…