5z55
NMR Solution Structure of the Kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)
Structural highlights
DiseaseROR1_HUMAN The disease is caused by mutations affecting the gene represented in this entry. FunctionROR1_HUMAN Has very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo (PubMed:25029443). Receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling (PubMed:25029443, PubMed:27162350). In inner ear, crucial for spiral ganglion neurons to innervate auditory hair cells (PubMed:27162350).[1] [2] Publication Abstract from PubMedReceptor 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. Backbone and side-chain chemical shift assignments of the kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1).,Ma X, Zhang Y, Liu B, Yang J, Hu K Biomol NMR Assign. 2018 Apr;12(1):145-148. doi: 10.1007/s12104-017-9797-9. Epub, 2018 Jan 8. PMID:29313214[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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