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5Z55

NMR Solution Structure of the Kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)

Summary for 5Z55
Entry DOI10.2210/pdb5z55/pdb
DescriptorInactive tyrosine-protein kinase transmembrane receptor ROR1 (1 entity in total)
Functional Keywordsror1, kringle, oncoprotein
Biological sourceHomo sapiens (Human)
Cellular locationMembrane ; Single-pass type I membrane protein: Q01973
Total number of polymer chains1
Total formula weight9562.52
Authors
Ma, X.,Hu, K.F. (deposition date: 2018-01-17, release date: 2018-05-16, Last modification date: 2024-10-23)
Primary citationMa, X.,Zhang, Y.,Liu, B.,Yang, J.,Hu, K.
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
Cited by
PubMed 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.
PubMed: 29313214
DOI: 10.1007/s12104-017-9797-9
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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