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Related Concept Videos

Protein Organization01:24

Protein Organization

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Conjugated Proteins02:50

Conjugated Proteins

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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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.
A protein's shape is critical to its function. For example, an enzyme...
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SARS-CoV-2 Spike Protein Post-Translational Modification Landscape and Its Impact on Protein Structure and Function

Buwen Liang1, Yiying Zhu2, Wenhao Shi2

  • 1The Hong Kong University of Science and Technology (Guangzhou), Guangzhou, China.

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This study maps 87 post-translational modifications (PTMs) on the SARS-CoV-2 spike protein. A novel mutagenesis approach combined with AlphaFold2 predicts PTM-influenced structures, revealing therapeutic targets.

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Area of Science:

  • Virology
  • Structural Biology
  • Computational Biology

Background:

  • Post-translational modifications (PTMs) significantly impact protein structure and function, yet are often overlooked in structure prediction.
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein's PTMs are crucial for its virulence and interaction with host factors.
  • Existing tools like AlphaFold2 primarily rely on amino acid sequences, neglecting PTM effects.

Purpose of the Study:

  • To elucidate the role of PTMs in SARS-CoV-2 spike protein structure and virulence.
  • To develop a computational method for predicting protein structures influenced by PTMs.
  • To analyze the impact of PTMs on spike protein interactions with host factors like angiotensin-converting enzyme 2 (ACE2).

Main Methods:

  • Generated a high-resolution map of 87 PTMs on SARS-CoV-2 spike protein using liquid chromatography-tandem mass spectrometry.
  • Proposed an in silico mutagenesis approach to mimic PTM effects by substituting amino acids.
  • Utilized AlphaFold2 with mutated sequences to predict PTM-altered spike protein structures.

Main Results:

  • Successfully mapped 87 PTMs on the SARS-CoV-2 spike protein.
  • The mutagenesis approach, coupled with AlphaFold2, accurately predicted PTM-influenced protein structures.
  • Computational analysis demonstrated that specific PTMs modulate the binding affinity of the spike protein to host factors like ACE2.

Conclusions:

  • PTMs critically influence SARS-CoV-2 spike protein structure and function.
  • The developed computational method provides novel insights into PTM-driven structural heterogeneity.
  • Targeting PTMs offers potential strategies for therapeutic interventions and antibody design against SARS-CoV-2.