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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

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 form...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Canonical Wnt Signaling Pathway02:54

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

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Related Experiment Video

Updated: Jun 3, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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

Published on: July 14, 2015

Structure and function of WD40 domain proteins.

Chao Xu1, Jinrong Min

  • 1Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, Ontario, Canada.

Protein & Cell
|April 7, 2011
PubMed
Summary

WD40 domains are abundant protein modules with a beta-propeller structure, crucial for diverse cellular processes by mediating protein-protein and protein-DNA interactions without enzymatic activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • WD40 domains are prevalent protein modules in eukaryotes, known for their role in protein-protein and protein-DNA interactions.
  • These domains adopt a conserved beta-propeller architecture, typically with seven blades.
  • They are implicated in a wide array of cellular functions.

Purpose of the Study:

  • To review the identification, definition, and structural architecture of WD40 domains.
  • To explore the diverse roles of WD40 domain proteins in cellular processes.
  • To discuss the molecular recognition mechanisms and binding modes of WD40 domains.

Main Methods:

  • Literature review of existing research on WD40 domains.
  • Analysis of structural data and protein interaction studies.

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Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
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Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

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Last Updated: Jun 3, 2026

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  • Compilation of information on functional roles and post-translational modification recognition.

    • Main Results:

    • WD40 domains possess a beta-propeller structure and function as interaction platforms.
    • They mediate molecular recognition through distinct surface areas.
    • No enzymatic activity has been associated with WD40 domains.

    Conclusions:

    • WD40 domains are versatile interaction modules critical for cellular regulation.
    • Understanding their structure and binding modes is key to deciphering their diverse functions.
    • Their role in recognizing post-translational modifications highlights their importance in signaling pathways.