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

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 targ...

Full description

Saved in:
Bibliographic Details
Published in:Biomolecular NMR assignments 2018-04, Vol.12 (1), p.145-148
Main Authors: Ma, Xiaofang, Zhang, Yingying, Liu, Bin, Yang, Jiahui, Hu, Kaifeng
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Apoptosis
Biochemistry
Biological and Medical Physics
Biophysics
Chronic lymphocytic leukemia
Humans
Leukemia
Lymphatic leukemia
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein-tyrosine kinase receptors
Receptor Tyrosine Kinase-like Orphan Receptors - chemistry
Therapeutic applications
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-017-9797-9