Backbone Flexibility Controls the Activity and Specificity of a Protein - Protein Interface: Specificity in Snake Venom Metalloproteases
2011
How Backbone Flexibility Affects Snake Venom Proteins
publication
Author Information
Author(s): Wallnoefer Hannes G, Lingott Torsten, Gutiérrez José María, Merfort Irmgard, Liedl Klaus R
Primary Institution: Institute of General, Inorganic and Theoretical Chemistry, Faculty of Chemistry and Pharmacy, University of Innsbruck
Hypothesis
The activity and specificity of snake venom metalloproteases (SVMPs) are influenced by the flexibility of their backbone structure.
Conclusion
The ability of SVMPs to induce hemorrhage is linked to the flexibility of specific regions in their structure.
Supporting Evidence
- Protein-protein interfaces are important for many biological functions.
- Snake venom metalloproteases (SVMPs) can bind to various proteins and cause bleeding.
- Some SVMPs are highly active in causing hemorrhage while others are nearly inactive despite similar sequences.
- The flexibility of certain loops in SVMPs is crucial for their ability to induce hemorrhage.
Takeaway
Some snake venom proteins can cause bleeding, and how flexible they are helps determine if they can do that.
Digital Object Identifier (DOI)
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