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7ODK

Plant peptide hormone receptor H1

This is a non-PDB format compatible entry.
Summary for 7ODK
Entry DOI10.2210/pdb7odk/pdb
DescriptorReceptor-like protein kinase HSL1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
Functional Keywordsplant receptor lrr pepide hormone, peptide binding protein
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Total number of polymer chains2
Total formula weight142981.98
Authors
Roman, A.O.,Jimenez-Sandoval, P.,Santiago, J. (deposition date: 2021-04-29, release date: 2022-02-16, Last modification date: 2024-11-20)
Primary citationRoman, A.O.,Jimenez-Sandoval, P.,Augustin, S.,Broyart, C.,Hothorn, L.A.,Santiago, J.
HSL1 and BAM1/2 impact epidermal cell development by sensing distinct signaling peptides.
Nat Commun, 13:876-876, 2022
Cited by
PubMed Abstract: The membrane receptor kinases HAESA and HSL2 recognize a family of IDA/IDL signaling peptides to control cell separation processes in different plant organs. The homologous HSL1 has been reported to regulate epidermal cell patterning by interacting with a different class of signaling peptides from the CLE family. Here we demonstrate that HSL1 binds IDA/IDL peptides with high, and CLE peptides with lower affinity, respectively. Ligand sensing capability and receptor activation of HSL1 require a SERK co-receptor kinase. Crystal structures with IDA/IDLs or with CLE9 reveal that HSL1-SERK1 complex recognizes the entire IDA/IDL signaling peptide, while only parts of CLE9 are bound to the receptor. In contrast, the receptor kinase BAM1 interacts with the entire CLE9 peptide with high affinity and specificity. Furthermore, the receptor tandem BAM1/BAM2 regulates epidermal cell division homeostasis. Consequently, HSL1-IDLs and BAM1/BAM2-CLEs independently regulate cell patterning in the leaf epidermal tissue.
PubMed: 35169143
DOI: 10.1038/s41467-022-28558-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.83 Å)
Structure validation

237992

数据于2025-06-25公开中

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