Biomolecular NMR Assignments

, Volume 12, Issue 1, pp 145–148 | Cite as

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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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.

Keywords

ROR1 Kringle NMR 

Notes

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).

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.

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© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  1. 1.State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of BotanyChinese Academy of SciencesKunmingPeople’s Republic of China
  2. 2.School of Basic MedicineChengdu University of TCMChengduPeople’s Republic of China

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