5Z55
NMR Solution Structure of the Kringle domain of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)
Summary for 5Z55
| Entry DOI | 10.2210/pdb5z55/pdb |
| Descriptor | Inactive tyrosine-protein kinase transmembrane receptor ROR1 (1 entity in total) |
| Functional Keywords | ror1, kringle, oncoprotein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Membrane ; Single-pass type I membrane protein: Q01973 |
| Total number of polymer chains | 1 |
| Total formula weight | 9562.52 |
| Authors | |
| Primary citation | Ma, 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: 29313214DOI: 10.1007/s12104-017-9797-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report






