ArticleProtein science : a publication of the Protein Society2018
Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 48 citations in OpenAlex.
- Malectin Alleviates Endoplasmic Reticulum Stress in Gestational Diabetes Mellitus via Glycoprotein Quality Control Mechanisms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The RALF-FERONIA Signaling Axis: A Central Hub Integrating Plant Growth, Reproduction, and Stress Responses.International journal of molecular sciences · 2025Review
- Three PP2C phosphatases modulate FERONIA receptor kinase activity to regulate pollen-stigma interaction in Arabidopsis.Plant communications · 2025Article
- FERONIA: A Receptor Kinase at the Core of a Global Signaling Network.Annual review of plant biology · 2024Review
- An update on evolutionary, structural, and functional studies of receptor-like kinases in plants.Frontiers in plant science · 2024Review
- Why is FERONIA pleiotropic?Nature plants · 2023Review
- Rapid alkalinization factor: function, regulation, and potential applications in agriculture.Stress biology · 2023Review
- Signals and Their Perception for Remodelling, Adjustment and Repair of the Plant Cell Wall.International journal of molecular sciences · 2023Review
- Growing Maize Root: Lectins Involved in Consecutive Stages of Cell Development.Plants (Basel, Switzerland) · 2022Article
- The Rice Malectin Regulates Plant Cell Death and Disease Resistance by Participating in Glycoprotein Quality Control.International journal of molecular sciences · 2022Article
- A plant receptor domain with functional analogies to animal malectin disables ER stress responses upon infection.iScience · 2022Article
- Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential.Cell surface (Amsterdam, Netherlands) · 2021Review
- Genome-wide identification and evolutionary analysis of RLKs involved in the response to aluminium stress in peanut.BMC plant biology · 2021Article
- A temperature-sensitive FERONIA mutant allele that alters root hair growth.Plant physiology · 2021Article
- Computational prediction method to decipher receptor-glycoligand interactions in plant immunity.The Plant journal : for cell and molecular biology · 2021Article
- Review
- RALF-FERONIA Signaling: Linking Plant Immune Response with Cell Growth.Plant communications · 2020Review
- Twenty Years of Progress in Physiological and Biochemical Investigation of RALF Peptides.Plant physiology · 2020Review
- CrRLK1L receptor-like kinases HERK1 and ANJEA are female determinants of pollen tube reception.EMBO reports · 2020Article
- Genome-Wide Identification ofFrontiers in plant science · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) proteins contain two tandem malectin-like modules in their extracellular domains (ECDs) and function in diverse signaling pathways in plants. Malectin is a carbohydrate-binding protein in animals and recognizes a number of diglucosides; however, it remains unclear how the two malectin-like domains in the CrRLK1L proteins sense the ligand molecule. In this study, we reveal the crystal structures of the ECDs of ANXUR1 and ANXUR2, two CrRLK1L members in Arabidopsis thaliana that have critical functions in controlling pollen tube rupture during the fertilization process. We show that the two malectin-like domains in these proteins pack together to form a rigid architecture. Unlike animal malectin, these malectin-like domains lack residues involved in binding to the diglucosides, suggesting that they have a distinct ligand-binding mechanism. A cleft is observed between the two malectin-like domains, which might function as a potential ligand-binding pocket.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.