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1H, 15N and 13C assignments of an intramolecular Lmo2-LIM2/Ldb1-LID complex

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Abstract

Lmo2 is a LIM-only protein involved in hematopoiesis and the development of T-cell acute lymphoblastic leukaemia. Here we report backbone and side chain NMR assignments for an engineered intramolecular complex of the C-terminal LIM domain from Lmo2 tethered to the LIM interaction domain (LID) from LIM domain binding protein 1 (Ldb1).

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References

  • Cheung MS, Maguire ML, Stevens TJ, Broadhurst RW (2010) DANGLE: a Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure. J Magn Reson 202:223–233

    Article  ADS  Google Scholar 

  • Deane JE, Mackay JP, Kwan AHY, Sum EYM, Visvader JE, Matthews JM (2003) Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4. EMBO J 22:2224–2233

    Article  Google Scholar 

  • Deane JE, Ryan DP, Sunde M, Maher MJ, Guss JM, Visvader JE, Matthews JM (2004) Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex. EMBO J 23:3589–3598

    Article  Google Scholar 

  • Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71–75

    Article  Google Scholar 

  • Nam CH, Rabbitts TH (2006) The role of LMO2 in development and in T cell leukemia after chromosomal translocation or retroviral insertion. Mol Ther 13:15–25

    Article  Google Scholar 

  • Pelton JG, Torchia DA, Meadow ND, Roseman S (1993) Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci 2:543–558

    Article  Google Scholar 

  • Ryan DP, Sunde M, Kwan AHY, Marianayagam NJ, Nancarrow AL, Hoven RNV, Thompson LS, Baca M, Mackay JP, Visvader JE, Matthews JM (2006) Identification of the key LMO2-binding determinants on Ldb1. J Mol Biol 359:66–75

    Article  Google Scholar 

  • Shen Y, Bax A (2007) Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology. J Biomol NMR 38:289–302

    Article  Google Scholar 

  • Vuister G, Bax A (1993) Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNHa) coupling constants in 15 N-enriched proteins. J Am Chem Soc 115:7772–7777

    Article  Google Scholar 

  • Yamazaki T, Froman-Kay J, Kay L (1993) Two-dimensional NMR experiments for correlating 13Cβ and 1Hδ/ε chemical shifts of aromatic residues in 13C-labelled proteins via scalar couplings. J Am Chem Soc 115:11054–11055

    Article  Google Scholar 

Download references

Acknowledgments

DPR was supported by an Australian Post Graduate Award, JPM and JMM were supported by senior research fellowships from the National Health and Medical Research Council of Australia (NHMRC). This work was supported by a project grant from the NHMRC.

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The authors declare they have no conflict of interest.

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Correspondence to Jacqueline M. Matthews.

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All experiments reported in this manuscript comply with the laws of Australia.

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Wilkinson-White, L.E., Dastmalchi, S., Kwan, A.H. et al. 1H, 15N and 13C assignments of an intramolecular Lmo2-LIM2/Ldb1-LID complex. Biomol NMR Assign 4, 203–206 (2010). https://doi.org/10.1007/s12104-010-9240-y

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  • DOI: https://doi.org/10.1007/s12104-010-9240-y

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