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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Related Experiment Video

Updated: Mar 11, 2026

Mutagenesis and Analysis of Genetic Mutations in the GC-rich KISS1 Receptor Sequence Identified in Humans with Reproductive Disorders
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mutLBSgeneDB: mutated ligand binding site gene DataBase.

Pora Kim1, Junfei Zhao1, Pinyi Lu1

  • 1Center for Precision Health, School of Biomedical Informatics, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.

Nucleic Acids Research
|December 2, 2016
PubMed
Summary
This summary is machine-generated.

Mutations in ligand binding sites (LBSs) are common in cancer. The new mutLBSgeneDB database catalogs these mutations, aiding research into drug resistance and protein function.

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Area of Science:

  • Genomics
  • Structural Biology
  • Pharmacology

Background:

  • Mutations in ligand binding sites (LBSs) impact protein stability, drug binding, and cancer drug resistance.
  • Ligand binding residues exhibit significantly higher mutation rates compared to other protein regions.

Purpose of the Study:

  • To develop mutLBSgeneDB, a comprehensive database of mutated ligand binding sites.
  • To provide a resource for analyzing LBS mutations in cancer and their functional implications.

Main Methods:

  • Curated over 2300 genes with approximately 12,000 somatic mutations in LBSs across 16 cancer types.
  • Integrated genetic, genomic, transcriptomic, proteomic, network, and functional data for analysis.
  • Developed a user-friendly web interface for data exploration.

Main Results:

  • Identified 744 drug-targetable genes with LBS mutations, including kinases, transcription factors, and cancer drivers.
  • Analyzed LBS mutation data, gene expression networks, drug response correlations, and protein stability.
  • Compared binding affinities of wild-type and mutant gene-drug pairs for 20 selected genes.

Conclusions:

  • mutLBSgeneDB serves as a valuable resource for functional genomics, protein structure, and drug discovery.
  • The database facilitates research into the impact of LBS mutations on cancer and therapeutic strategies.