ArticleProtein science : a publication of the Protein Society1995
Crystal structure of human pepsin and its complex with pepstatin.
Article in Protein science : a publication of the Protein Society, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 139 citations in OpenAlex.
- A tool for predicting pH and temperature effects on porcine and human pepsin activity during in vitro gastric digestion.Scientific reports · 2026Article
- Structural determinants for pH-dependent activation of a plant metacaspase.Nature communications · 2025Article
- Familial Alzheimer mutations stabilize synaptotoxic γ-secretase-substrate complexes.Cell reports · 2024Article
- AlphaFold-Multimer predicts cross-kingdom interactions at the plant-pathogen interface.Nature communications · 2023Article
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification inFrontiers in plant science · 2023Article
- Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy.Nature communications · 2022Article
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- AnACS catalysis · 2019Article
- Gastric cancer and Hedgehog signaling pathway: emerging new paradigms.Genes & cancer · 2018Review
- BACE1 Function and Inhibition: Implications of Intervention in the Amyloid Pathway of Alzheimer's Disease Pathology.Molecules (Basel, Switzerland) · 2017Review
- Hedgehog Signaling Links Chronic Inflammation to Gastric Cancer Precursor Lesions.Cellular and molecular gastroenterology and hepatology · 2017Review
- Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion.Beilstein journal of organic chemistry · 2017Article
- Alginate as a protease inhibitor in vitro and in a model gut system; selective inhibition of pepsin but not trypsin.Carbohydrate polymers · 2015Article
- Crystal structure of a putative aspartic proteinase domain of the Mycobacterium tuberculosis cell surface antigen PE_PGRS16.FEBS open bio · 2013Article
- Aspartic peptidases of human pathogenic trypanosomatids: perspectives and trends for chemotherapy.Current medicinal chemistry · 2013Review
- Dynamics of thermodynamically stable, kinetically trapped, and inhibitor-bound states of pepsin.Biophysical journal · 2011Article
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- Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation.Journal of medicinal chemistry · 2009Article
- Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.Proteins · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The three-dimensional crystal structure of human pepsin and that of its complex with pepstatin have been solved by X-ray crystallographic methods. The native pepsin structure has been refined with data collected to 2.2 A resolution to an R-factor of 19.7%. The pepsin:pepstatin structure has been refined with data to 2.0 A resolution to an R-factor of 18.5%. The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic proteinases. The enzyme undergoes a conformational change upon inhibitor binding to enclose the inhibitor more tightly. The analysis of the binding sites indicates that they form an extended tube without distinct binding pockets. By comparing the residues on the binding surface with those of the other human aspartic proteinases, it has been possible to rationalize some of the experimental data concerning the different specificities. At the S1 site, valine at position 120 in renin instead of isoleucine, as in the other enzymes, allows for binding of larger hydrophobic residues. The possibility of multiple conformations for the P2 residue makes the analysis of the S2 site difficult. However, it is possible to see that the specific interactions that renin makes with histidine at P2 would not be possible in the case of the other enzymes. At the S3 site, the smaller volume that is accessible in pepsin compared to the other enzymes is consistent with its preference for smaller residues at the P3 position.
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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.