GRE4Zn

GRE4Zn characterizes zinc-binding sites in protein structures by applying geometric distance restrictions between zinc ions and coordinating atoms to identify and distinguish 3-residue and 4-residue coordination sites relevant to transcription regulation, cell metabolism, and apoptosis.


Key Features:

  • Geometric analysis: GRE4Zn systematically analyzes structural characteristics to identify distinct geometric features associated with 3-residue and 4-residue zinc-binding sites.
  • Distance restriction methodology: The program restricts distances between zinc ions and their coordinating atoms to enhance the accuracy of site characterization.
  • Comparative performance: Comparative studies have demonstrated that GRE4Zn predicts zinc-binding sites with higher precision than analogous tools.

Scientific Applications:

  • Biological function elucidation: Accurate characterization of zinc-binding sites aids in elucidating molecular mechanisms and biological functions of zinc-binding proteins.
  • Evolutionary insights: Large-scale predictions using GRE4Zn reveal increasing involvement of zinc-binding proteins in complex biological processes across evolution from simpler to higher organisms.
  • Disease association and drug targeting: Analyses indicate zinc-binding proteins are preferentially implicated in various diseases and are highly enriched among known drug targets, supporting investigation of disease mechanisms and drug design.

Methodology:

GRE4Zn is based on the observation that specific geometric features define 3-residue and 4-residue zinc-binding sites and restricts distances between zinc ions and coordinating atoms to predict binding sites in protein structures.

Topics

Details

Tool Type:
web application
Operating Systems:
Linux, Windows, Mac
Added:
8/3/2017
Last Updated:
11/25/2024

Operations

Publications

Liu Z, Wang Y, Zhou C, Xue Y, Zhao W, Liu H. Computationally characterizing and comprehensive analysis of zinc-binding sites in proteins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2014;1844(1):171-180. doi:10.1016/j.bbapap.2013.03.001. PMID:23499845.

Documentation

Links