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  • Oral presentation
  • Open Access

Backbone flexibility controls the activity and specificity of a protein-protein interface – specificity in snake venom metalloproteases (SVMPs)

  • 1,
  • 2,
  • 3,
  • 2 and
  • 1Email author
Journal of Cheminformatics20113 (Suppl 1) :O22

  • Published:


  • Basement Membrane
  • Significant Alteration
  • Surface Region
  • Damage Function
  • Potential Reaction

Protein-Protein interfaces have crucial functions in many biological processes [1]. The large interaction areas of such interfaces show complex interaction motifs. Even more challenging is the understanding of (multi-)specificity in protein-protein binding. Many proteins can bind several partners to mediate their function [2].

A perfect paradigm to study such multi-specific protein-protein interfaces are snake venom metalloproteases (SVMPs) [3]. Inherently, they bind to a variety of basement membrane proteins of capillaries, hydrolyze them, and induce profuse bleeding. However, despite having a high sequence homology, some SVMPs show a strong hemorrhagic activity, while others are (almost) inactive [4].

Our results indicate that the activity to induce hemorrhage, and thus the capability to bind the potential reaction partners, is related to the backbone flexibility in a certain surface region[4]. A subtle interplay between flexibility and rigidity of two loops seems to be the prerequisite for the proteins to carry out their damaging function. Presumably, a significant alteration in the backbone dynamics makes the difference between SVMPs that induce hemorrhage and the inactive ones.

Authors’ Affiliations

Institute of General, Inorganic and Theoretical Chemistry, Faculty of Chemistry and Pharmacy, University of Innsbruck, Innsbruck, 6020, Austria
Institute of Pharmaceutical Sciences, Department of Pharmaceutical Biology and Biotechnology, University of Freiburg, 79104 Freiburg, Germany
Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica


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© Wallnoefer et al; licensee BioMed Central Ltd. 2011

This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.