ArticleThe Journal of biological chemistry2016
Crystal Structure of Human Leukocyte Cell-derived Chemotaxin 2 (LECT2) Reveals a Mechanistic Basis of Functional Evolution in a Mammalian Protein with an M23 Metalloendopeptidase Fold.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Key Hepatokines Linking MASLD and Type 2 Diabetes: From Pathophysiological Mechanisms to Therapeutic Modulation.International journal of molecular sciences · 2026Review
- The long road to recognition: a historical review of amyloidosis from early pathology to disease-modifying therapy.Heart failure reviews · 2026Review
- Cryo-EM structures of ALECT2 filaments from human renal biopsies.Nature communications · 2026Article
- Cryo-EM structure of a human LECT2 amyloid fibril reveals a network of polar ladders at its core.Structure (London, England : 1993) · 2023Article
- Cryo-EM Structure of a Human LECT2 Amyloid Fibril Reveals a Network of Polar Ladders at its Core.bioRxiv : the preprint server for biology · 2023Article
- The emerging roles of leukocyte cell-derived chemotaxin-2 in immune diseases: From mechanisms to therapeutic potential.Frontiers in immunology · 2023Review
- LECT2: A pleiotropic and promising hepatokine, from bench to bedside.Journal of cellular and molecular medicine · 2022Review
- Organokines in Rheumatoid Arthritis: A Critical Review.International journal of molecular sciences · 2022Review
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase.International journal of molecular sciences · 2021Article
- LECT2 Protects Nile Tilapia (Frontiers in immunology · 2021Article
- Alleviation of lipopolysaccharide/d-galactosamine-induced liver injury in leukocyte cell-derived chemotaxin 2 deficient mice.Biochemistry and biophysics reports · 2017Article
- Laminarinase from Flavobacterium sp. reveals the structural basis of thermostability and substrate specificity.Scientific reports · 2017Article
- Leukocyte Cell-Derived Chemotaxin-2: It's Role in Pathophysiology and Future in Clinical Medicine.Clinical and translational science · 2017Review
- Loss of bound zinc facilitates amyloid fibril formation of leukocyte-cell-derived chemotaxin 2 (LECT2).The Journal of biological chemistryArticle
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Authors and funding
7 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Human leukocyte cell-derived chemotaxin 2 (LECT2), which is predominantly expressed in the liver, is a multifunctional protein. LECT2 is becoming a potential therapeutic target for several diseases of worldwide concern such as rheumatoid arthritis, hepatocellular carcinoma, and obesity. Here, we present the crystal structure of LECT2, the first mammalian protein whose structure contains an M23 metalloendopeptidase fold. The LECT2 structure adopts a conserved Zn(II) coordination configuration but lacks a proposed catalytic histidine residue, and its potential substrate-binding groove is blocked in the vicinity of the Zn(II)-binding site by an additional intrachain loop at the N terminus. Consistent with these structural features, LECT2 was found to be catalytically inactive as a metalloendopeptidase against various types of peptide sequences, including pentaglycine. In addition, a surface plasmon resonance analysis demonstrated that LECT2 bound to the c-Met receptor with micromolar affinity. These results indicate that LECT2 likely plays its critical roles by acting as a ligand for the corresponding protein receptors rather than as an enzymatically active peptidase. The intrachain loop together with the pseudo-active site groove in LECT2 structure may be specific for interactions between LECT2 and receptors. Our study reveals a mechanistic basis for the functional evolution of a mammalian protein with an M23 metalloendopeptidase fold and potentially broadens the implications for the biological importance of noncatalytic peptidases in the M23 family.
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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.