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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
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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.
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Laser-free Hydroxyl Radical Protein Footprinting to Perform Higher Order Structural Analysis of Proteins
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Structure of Zona Pellucida Module Proteins.

Marcel Bokhove1, Luca Jovine1

  • 1Department of Biosciences and Nutrition & Center for Innovative Medicine, Karolinska Institutet, Huddinge, Sweden.

Current Topics in Developmental Biology
|June 2, 2018
PubMed
Summary

The egg coat

Area of Science:

  • Structural biology
  • Reproductive biology
  • Biochemistry

Background:

  • The egg coat, a glycoprotein matrix, is vital for fertilization, controlling sperm entry.
  • Its components utilize a zona pellucida (ZP) domain, comprising ZP-N and ZP-C immunoglobulin-like domains, for polymerization.
  • Mutations in ZP domain-containing proteins are linked to severe human diseases.

Purpose of the Study:

  • To review recent advances in understanding the ZP module's atomic architecture and polymerization.
  • To explore the structural basis of sperm-egg coat interactions.
  • To highlight the link between invertebrate and vertebrate fertilization mechanisms.

Main Methods:

  • Structural analysis of ZP domains and their polymerization.
  • Investigation of sperm-binding regions in egg coat proteins.
Keywords:
Endoglin–BMP9 complexFertilizationUromodulinVERL–lysin complexX-ray crystallographyZP domainZP moduleZP-C domainZP-N domainZP1ZP2ZP3ZP4Zona pellucida

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  • Comparative analysis of ZP module structures across species.

    • Main Results:

    • Significant progress in elucidating the ZP module's atomic structure and polymerization mechanisms.
    • Identification of ZP-N fold in sperm-binding regions of invertebrate and vertebrate egg coat proteins.
    • Determination of the first structure of an egg coat-sperm protein recognition complex.

    Conclusions:

    • The ZP module is a conserved structural unit involved in fertilization across diverse species.
    • Understanding ZP module structure provides insights into reproductive processes and disease mechanisms.
    • Further research is needed for a comprehensive view of ZP domain-containing proteins.