ArticleNature structural biology1997
Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding.
Article in Nature structural biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 191 citations in OpenAlex.
- Calpain small subunit homodimerization is robust and calcium-independent.FEBS letters · 2026Article
- A workflow to create a high-quality protein-ligand binding dataset for training, validation, and prediction tasks.Digital discovery · 2025Article
- Article
- Signal Peptides and Their Fragments in Post-Translation: Novel Insights of Signal Peptides.International journal of molecular sciences · 2024Review
- Human calpain-3 and its structural plasticity: dissociation of a homohexamer into dimers on binding titin.bioRxiv : the preprint server for biology · 2024Article
- Calpain-mediated proteolysis as driver and modulator of polyglutamine toxicity.Frontiers in molecular neuroscience · 2022Review
- Structural and functional diversity of EF-hand proteins: Evolutionary perspectives.Protein science : a publication of the Protein Society · 2017Review
- Calpain research for drug discovery: challenges and potential.Nature reviews. Drug discovery · 2016Review
- Conformationally restricted calpain inhibitors.Chemical science · 2015Article
- Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors.Acta pharmaceutica Sinica. B · 2015Review
- Membrane Repair: Mechanisms and Pathophysiology.Physiological reviews · 2015Review
- Understanding the interaction determinants of CAPN1 inhibition by CAST4 from bovines using molecular modeling techniques.Molecules (Basel, Switzerland) · 2014Article
- Calpain system and its involvement in myocardial ischemia and reperfusion injury.World journal of cardiology · 2014Review
- Homology modeling study of bovine μ-calpain inhibitor-binding domains.International journal of molecular sciences · 2014Article
- A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review.Asian-Australasian journal of animal sciences · 2013Review
- Calcium, calpain, and calcineurin in low-frequency depression of transmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Calpains, mitochondria, and apoptosis.Cardiovascular research · 2012Review
- Characterization of the 1st and 2nd EF-hands of NADPH oxidase 5 by fluorescence, isothermal titration calorimetry, and circular dichroism.Chemistry Central journal · 2012Article
- The atypical calpains: evolutionary analyses and roles in Caenorhabditis elegans cellular degeneration.PLoS genetics · 2012Article
- Nox5 forms a functional oligomer mediated by self-association of its dehydrogenase domain.Biochemistry · 2011Article
Corrections and comments
- Commented on by
Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three dimensional structure of calcium-bound domain VI of porcine calpain has been determined to 1.9 A resolution. The crystal structure reveals five EF-hands, one more than previously suggested. There are two EF-hand pairs, one pair (EF1-EF2) displays an 'open' conformation and the other (EF3-EF4) a 'closed' conformation. Unusually, a calcium atom is found at the C-terminal end of the calcium binding loop of EF4. With two additional residues in the calcium binding loop, the fifth EF-hand (EF5) is in a 'closed' conformation. EF5 pairs up with the corresponding fifth EF-hand of a non-crystallographically related molecule. Considering the EF5's role in a homodimer formation of domain VI, we suggest a model for the assembly of heterodimeric calpain. The crystal structure of a Ca2+ bound domain VI-inhibitor (PD150606) complex has been refined to 2.1 A resolution. A possible mode for calpain inhibition is discussed.
Indexed as
Identifiers
What 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.