Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP

@article{PrezAlvarado1994StructureOT,
  title={Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP},
  author={Gabriela C. P{\'e}rez-Alvarado and Colleen Miles and James W. Michelsen and Heather A. Louis and Dennis R Winge and Mary C Beckerle and Michael F Summers},
  journal={Nature Structural Biology},
  year={1994},
  volume={1},
  pages={388-398}
}
The three dimensional solution structure of the carboxy terminal LIM domain of the avian Cysteine Rich Protein (CRP) has been determined by nuclear magnetic resonance spectroscopy. The domain contains two zinc atoms bound independently in CCHC (C=Cys, H=His) and CCCC modules. Both modules contain two orthogonally-arranged antiparallel β-sheets, and the CCCC module contains an α-helix at its C terminus. The modules pack due to hydrophobic interactions forming a novel global fold. The structure… CONTINUE READING

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