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Backbone and side-chain chemical shift assignments of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)

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A Correction to this article was published on 28 June 2018

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Abstract

Receptor tyrosine kinase-like orphan receptor 1 (ROR1) expresses at high level in many cancers and has been suggested as a potential therapeutic target. It was reported that the Kringle (KNG) domain of ROR1 extracellular region is involved in ROR1/ROR2 heterooligomerization. Monoantibodies that target KNG domain of ROR1 could induce apoptosis of chronic lymphocytic leukemia cells. Here we present the backbone and side chain assignments of KNG domain of ROR1, which lays a foundation for its further structural and function research.

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  • 28 June 2018

    The authors would like to include an additional institution to their affiliation which was initially not included in the original publication of the article

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Acknowledgements

This work was supported by the National Key Research and Development Program of China (No. 2017YFC0906903), the National Natural Science Foundation of China (No. 81401904, 31400642) and Yunnan Provincial Science and Technology Department (No. 2015FB170).

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Correspondence to Jiahui Yang or Kaifeng Hu.

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Ma, X., Zhang, Y., Liu, B. et al. Backbone and side-chain chemical shift assignments of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1). Biomol NMR Assign 12, 145–148 (2018). https://doi.org/10.1007/s12104-017-9797-9

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  • DOI: https://doi.org/10.1007/s12104-017-9797-9

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