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Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses
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Published on: November 3, 2014

Structure-function inferences based on molecular modeling, sequence-based methods and biological data analysis of

Paula Alvarez Abreu1, Magaly Girão Albuquerque, Carlos Rangel Rodrigues

  • 1Laboratório de Bioquímica e Modelagem Molecular, Departamento de Biologia Celular e Molecular, Instituto de Biologia, CEG, Universidade Federal Fluminense, CEP 24001-970, Niterói, RJ, Brazil.

Toxicon : Official Journal of the International Society on Toxinology
|October 19, 2006
PubMed
Summary

Snake venom lectins (SVLs) possess unique structural features, including a specific disulfide bond and a reoriented loop, aiding carbohydrate binding. These theoretical models reveal insights into SVL function and interactions.

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Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group

Published on: August 16, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Venomics

Background:

  • Lectins are diverse proteins that bind carbohydrates; snake venom lectins (SVLs) are calcium-dependent and recognize galactose.
  • Understanding the structure-function relationships of SVLs is crucial for deciphering their biological roles.

Purpose of the Study:

  • To construct theoretical models of 10 SVLs based on the Crotalus atrox lectin (CaL) structure.
  • To compare these SVL models with other lectins and C-type lectin-like proteins (CLPs) to identify unique features.

Main Methods:

  • Theoretical modeling of 10 snake venom lectins (SVLs).
  • Comparative analysis with existing crystal structures of CaL, other animal and plant lectins, and C-type lectin-like proteins (CLPs).

Main Results:

  • Identified a unique intrachain disulfide bond (Cys(38)-Cys(133)) in SVLs, absent in CLPs.
  • Observed a significant reorientation of the 80's loop, crucial for carbohydrate recognition and dimer formation.
  • Characterized the carbohydrate recognition domain (CRD) with a negatively charged, concave surface for saccharide and calcium ion interaction.
  • Noted the role of water molecules in interchain interactions, similar to other lectins.
  • Found SVLs generally unable to form oligomers, unlike CaL and some CLPs.

Conclusions:

  • Theoretical models reveal distinct structural characteristics of SVLs, including a unique disulfide bond and loop reorientation.
  • These features contribute to the specific carbohydrate-binding capabilities and interactions of SVLs.
  • SVLs exhibit differences in oligomerization compared to other lectins and CLPs.