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Related Concept Videos

Catenins01:23

Catenins

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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Cytoskeletal Accessory Proteins01:13

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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Cystatins: a versatile family.

Veronica Esposito, Piero A Temussi

    Biomolecular Concepts
    |May 12, 2015
    PubMed
    Summary

    Cystatins are proteins with diverse functions, including protease inhibition, aggregation in diseases, and eliciting sweet taste. Their aggregation mechanisms, particularly 3D domain swapping, are crucial for understanding misfolding diseases.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Cystatins are a superfamily of small proteins (100-120 amino acids) with diverse biological roles.
    • Beyond protease inhibition, cystatins exhibit aggregation properties linked to misfolding diseases and unique taste-modulating functions, exemplified by the plant cystatin monellin.

    Purpose of the Study:

    • To explore the multifaceted roles of cystatins, focusing on their aggregation mechanisms and the sweet taste phenomenon.
    • To elucidate the structural basis for monellin's sweet taste and high thermal stability.
    • To investigate the aggregation pathways of cystatins, including those related to misfolding diseases and engineered sweet proteins.

    Main Methods:

    • Structural studies of monellin to understand its thermal stability and taste properties.

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  • Analysis of cystatin aggregation mechanisms, with a focus on 3D domain swapping.
  • Comparative study of aggregation pathways in naturally occurring and engineered cystatins.

    • Main Results:

    • Monellin's unique sweet taste and thermal stability were investigated through in-depth structural analysis.
    • Cystatin aggregation mechanisms, particularly 3D domain swapping, were detailed and linked to misfolding diseases.
    • Monellin aggregates via a conventional cross-β spine mechanism, while engineered cystatins exhibit distinct aggregation pathways.

    Conclusions:

    • Cystatins possess diverse functionalities extending beyond protease inhibition.
    • Understanding cystatin aggregation is vital for research into misfolding diseases.
    • The study provides insights into the structural basis of sweet taste in proteins and the mechanisms of protein aggregation.