7brc | pdb_00007brc
Crystal structure of the TMK3 LRR domain
Structural highlights
FunctionTMK3_ARATH Involved in auxin signal transduction and cell expansion and proliferation regulation (PubMed:23613767).[1] Publication Abstract from PubMedTransmembrane kinases (TMKs) are members of the plant receptor-like kinase (RLK) family. TMKs are characterized by an extracellular leucine-rich-repeat (LRR) domain, a single transmembrane region and a cytoplasmic kinase domain. TMKs have been shown to act as critical modulators of cell expansion and cell proliferation. Here, the crystal structure of the extracellular domain of TMK3 (TMK3-ECD) was determined to a resolution of 2.06 A, with an Rwork of 17.69% and an Rfree of 20.58%. Similar to the extracellular domain of TMK1, the TMK3-ECD structure contains two solenoids with 13 LRRs and a non-LRR region (316-364) between the tenth and 11th LRRs. A comparison of TMK3-ECD with other LRR-RLKs that contain a non-LRR region indicates that the non-LRR region plays a critical role in structural integrity and may contribute to ligand interactions. The non-LRR region of TMK3-ECD is characterized by two disulfide bonds that may have critical biological implications. Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.,Chen H, Kong Y, Chen J, Li L, Li X, Yu F, Ming Z Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):384-390. doi:, 10.1107/S2053230X20010122. Epub 2020 Jul 29. PMID:32744250[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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