ArticleThe EMBO journal1996
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
123 citing papers in PubMed, 390 citations in OpenAlex.
- Cathepsin L as a Driver of Tumour Invasion and a Novel Therapeutic Target in Ovarian Cancer.Cancers · 2026Review
- To Explore Potential Natural Inhibitors of Cysteine Proteases to Combat Human African Trypanosomiasis and Chagas Disease.Current medicinal chemistry · 2026Review
- Article
- Machine learning models for prediction of (Pro)cathepsin-glycosaminoglycan binding free energies based on molecular structure.Computational and structural biotechnology journal · 2026Article
- Production of human cathepsins using Expi293™ mammalian cell expression system for off-target activity of cysteine protease inhibitor screening.Protein science : a publication of the Protein Society · 2025Article
- Evaluating the protonation state of the catalytic Cys25 in cruzain cysteine protease: A target for Chagas disease.Protein science : a publication of the Protein Society · 2025Article
- 1,2,4-Thiadiazolidin-3,5-Diones as Inhibitors of Cysteine Proteases.Molecules (Basel, Switzerland) · 2025Article
- Article
- Genome-wide association for multiple quantitative traits in forage oat germplasm based on specific length amplified fragment sequencing.Frontiers in plant science · 2025Article
- Cysteine protease I29 propeptide from Calotropis procera R. Br. As a potent cathepsin L inhibitor and its suppressive activity in breast cancer metastasis.Scientific reports · 2024Article
- Structure-based design of pan-coronavirus inhibitors targeting host cathepsin L and calpain-1.Signal transduction and targeted therapy · 2024Article
- Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis.Parasite (Paris, France) · 2024Article
- Targeting Cysteine Proteases and their Inhibitors to Combat Trypanosomiasis.Current medicinal chemistry · 2024Review
- Structure-based discovery of dual pathway inhibitors for SARS-CoV-2 entry.Nature communications · 2023Article
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS.Nature communications · 2022Article
- Molecular characterization and determination of the biochemical properties of cathepsin L of Trichinella spiralis.Veterinary research · 2022Article
- Article
- Different Genes are Recruited During Convergent Evolution of Pregnancy and the Placenta.Molecular biology and evolution · 2022Article
- Characterization and molecular docking study of cathepsin L inhibitory peptides (SnuCalCpIs) from Calotropis procera R. Br.Scientific reports · 2022Article
63 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cathepsin L is a member of the papain superfamily of cysteine proteases and, like many other proteases, it is synthesized as an inactive proenzyme. Its prosegment shows little homology to that of procathepsin B, whose structure, the first for a cysteine protease proenzyme, has been determined recently. We report here the 3-D structure of a mutant of human procathepsin L determined at 2.2 A resolution, describe the mode of binding employed by the prosegment and discuss the molecular basis for other possible roles of the prosegment. The N-terminal part of the prosegment is globular and contains three alpha-helices with a small hydrophobic core built around aromatic side chains. This domain packs against a loop on the enzyme's surface, with the aromatic side chain from the prosegment being located in the center of this loop and providing a large contact area. The C-terminal portion of the prosegment assumes an extended conformation and follows along the substrate binding cleft toward the N-terminus of the mature enzyme. The direction of the prosegment in the substrate binding cleft is opposite to that of substrates. The previously described role of the prosegment in the interactions with membranes is supported by the structure of its N-terminal domain. The fold of the prosegment and the mechanism by which it inhibits the enzymatic activity of procathepsin L is similar to that observed in procathepsin B despite differences in length and sequence, suggesting that this mode of inhibition is common to all enzymes from the papain superfamily.
Indexed as
Identifiers
8896443PMC452294W1920417980What OpenQuestion holds
Registered trials
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.