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Ligand Binding Sites

Ligand Binding Sites

Ligand Binding Sites

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding and Linkage

Ligand Binding and Linkage

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...

Ligand Binding and Linkage

Ligand Binding and Linkage

Selectins

Selectins

Cell adhesion is an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Related Experiment Video

Updated: Dec 23, 2025

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Structural Database for Lectins and the UniLectin Web Platform.

François Bonnardel^1,2,3, Serge Perez¹, Frédérique Lisacek^4,5,6

¹Univ. Grenoble Alpes, CNRS, CERMAV, Grenoble, France.

Methods in Molecular Biology (Clifton, N.J.)

|April 20, 2020

Summary

This summary is machine-generated.

UniLectin is a new platform that provides insights into lectins, proteins that bind to glycans. It offers a classification, 3D structures, and tools for predicting lectin diversity and function.

Keywords:

3D structure Carbohydrate-binding protein Classification Database Lectin Profile-based prediction Sequence

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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

Published on: October 1, 2009

Area of Science:

Biochemistry
Structural Biology
Bioinformatics

Background:

Glycans are poorly characterized biomolecules crucial for biological processes.
Lectins, proteins that bind glycans, play significant roles in cell recognition and interactions.
Existing lectin databases have limited connectivity with major omics databases.

Purpose of the Study:

To introduce UniLectin, a novel platform for exploring lectin knowledge.
To provide a flexible classification system for diverse lectin sequences and structures.
To develop tools for predicting lectin function and diversity.

Main Methods:

Development of UniLectin platform, including UniLectin3D database of curated lectin 3D structures.
Implementation of a periodically updated lectin classification system.
Creation of the PropLec module for predicting beta-propeller lectins using family profiles.

Main Results:

UniLectin integrates lectin 3D structures, classification, and comparative tools.
The platform facilitates exploration of lectin diversity and biological roles.
PropLec enables reliable prediction of beta-propeller lectins across species.

Conclusions:

UniLectin enhances understanding of lectin diversity, structure, and function.
The platform addresses the need for integrated and updated lectin information.
UniLectin provides valuable tools for lectin research and prediction.