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Updated: Aug 14, 2026
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High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
Viper venom disintegrins and related molecules
M A McLane1, C Marcinkiewicz, S Vijay-Kumar
1Department of Medical Technology, University of Delaware, Newark 19716, USA.
Summary
Disintegrins are small proteins from viper venom that interact with integrin receptors. Research now shows related domains in other proteins, expanding their study.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Disintegrins, first identified in 1990, are nonenzymatic proteins from viper venom.
- They exhibit sequence homology and variable potency/selectivity in binding integrin receptors.
- Related disintegrin-like domains are found in larger mosaic proteins and other species.
Purpose of the Study:
- To review the literature on disintegrin structure and function.
- To discuss the authors' data on disintegrins.
- To explore the relevance of disintegrins to proteins with disintegrin-like domains.
Main Methods:
- Literature review of scientific publications.
- Analysis of authors' experimental data (details not specified in abstract).
- Comparative analysis of disintegrins and related protein domains.
Main Results:
- Disintegrins share structural and functional properties, interacting with integrin receptors.
- Variability in disintegrin potency and selectivity is noted.
- Disintegrin-like domains are present in diverse proteins, including hemorrhagins and ADAMs.
Conclusions:
- Disintegrins are a significant class of bioactive proteins with implications beyond viper venom.
- The study of disintegrins and related domains is crucial for understanding protein-receptor interactions.
- Further research is warranted on the diverse roles of disintegrin-like domains in biological systems.
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