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Conservation of Protein Domains

Conservation of Protein Domains

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Protein Families

Protein Families

Protein Families

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

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Updated: Apr 21, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

WDSPdb: a database for WD40-repeat proteins.

Yang Wang¹, Xue-Jia Hu¹, Xu-Dong Zou¹

¹Lab of Computational Chemistry and Drug Design, Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, 518055, P. R. China.

Nucleic Acids Research

|October 29, 2014

Summary

This summary is machine-generated.

Researchers can now access WDSPdb, a new database detailing WD40-repeat proteins. This resource provides structural information and potential interaction sites, aiding studies on protein function and interactions.

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Last Updated: Apr 21, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Published on: July 14, 2015

An Integrated Approach for Microprotein Identification and Sequence Analysis

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Published on: July 12, 2022

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Area of Science:

Biochemistry
Structural Biology
Bioinformatics

Background:

WD40-repeat proteins are a large family crucial for biological processes, acting as platforms for complex assembly via hotspot residues.
Understanding the structure and interaction sites of WD40 domains is essential for researchers studying these proteins and their roles in protein-protein interactions.
Existing resources may lack comprehensive structural and interaction data for the vast number of WD40-repeat proteins.

Purpose of the Study:

To systematically identify WD40-repeat proteins and predict their structural and functional features.
To develop a specialized database, WDSPdb, offering detailed information on WD40-repeat proteins.
To provide researchers with a valuable resource for studying WD40 protein structures and interaction hotspots.

Main Methods:

Developed the WDSPdb database, utilizing the recently published WDSP method.
Systematically identified 63,211 WD40-repeat proteins from 3,383 species.
Implemented a user-friendly web interface for data browsing, searching, and downloading.

Main Results:

WDSPdb provides comprehensive data for 63,211 WD40-repeat proteins across 3,383 species.
Includes predictions for secondary structures, tertiary structure models, and potential hotspot residues.
The database covers most well-known model organisms, enhancing its utility.

Conclusions:

WDSPdb serves as a valuable resource for the scientific community studying WD40-repeat proteins.
The database facilitates research on protein structure, function, and protein-protein interactions.
The user-friendly interface enables easy access to critical structural and interaction data.