ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of human ADAM-8 catalytic domain complexed with batimastat.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Metal binding site alignment enables network-driven discovery of recurrent geometries across sequence-divergent proteins and drug off-targets.PLoS computational biology · 2026Article
- Article
- A Novel Class of Human ADAM8 Inhibitory Antibodies for Treatment of Triple-Negative Breast Cancer.Pharmaceutics · 2024Article
- Developments in Carbohydrate-Based Metzincin Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2020Review
- ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview.Toxins · 2016Review
- Evidence for restricted reactivity of ADAMDEC1 with protein substrates and endogenous inhibitors.The Journal of biological chemistry · 2015Article
- Fibronectin fragments and the cleaving enzyme ADAM-8 in the degenerative human intervertebral disc.Spine · 2014Article
- Genetically Engineered Mouse Models Reveal the Importance of Proteases as Osteoarthritis Drug Targets.Current rheumatology reports · 2013Review
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
The role of ADAM-8 in cancer and inflammatory diseases such as allergy, arthritis and asthma makes it an attractive target for drug development. Therefore, the catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme-inhibitor complex was refined to 2.1 Å resolution. ADAM-8 has an overall fold similar to those of other ADAM members, including a central five-stranded β-sheet and a catalytic Zn(2+) ion. However, unique differences within the S1' binding loop of ADAM-8 are observed which might be exploited to confer specificity and selectivity to ADAM-8 competitive inhibitors for the treatment of diseases involving this enzyme.
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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.