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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.
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Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
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Single Nucleotide Polymorphisms-SNPs

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A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...

Genome-wide Association Studies-GWAS

Genome-wide Association Studies-GWAS

Genome-wide association studies or GWAS are used to identify whether common SNPs are associated with certain diseases. Suppose specific SNPs are more frequently observed in individuals with a particular disease than those without the disease. In that case, those SNPs are said to be associated with the disease. Chi-square analysis is performed to check the probability of the allele likely to be associated with the disease.
GWAS does not require the identification of the target gene involved in...

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Related Experiment Video

Updated: Apr 7, 2026

Determining the Likelihood of Variant Pathogenicity Using Amino Acid-level Signal-to-Noise Analysis of Genetic Variation

Determining the Likelihood of Variant Pathogenicity Using Amino Acid-level Signal-to-Noise Analysis of Genetic Variation

Published on: January 16, 2019

Amino acid repeat signatures underlying human-pathogen interactions.

Anjali Kumari Singh¹, Nagashree Rachote¹, Vaidehi Sharma¹

¹Department of Biology, Indian Institute of Science Education and Research (IISER) Tirupati, Tirupati 517619, Andhra Pradesh, India.

|April 6, 2026

Summary

This summary is machine-generated.

Pathogens interact with human proteins containing amino acid homorepeats (HRs) to affect host processes. Different pathogen types utilize distinct HR strategies for host engagement, impacting infection outcomes.

Keywords:

computational bioinformatics microbiology molecular biology

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Area of Science:

Biochemistry
Molecular Biology
Pathogen-Host Interactions

Background:

Amino acid homorepeats (HRs) within human proteins (HRPs) are increasingly recognized for their role in protein interactions.
Understanding how pathogens exploit HRPs is crucial for deciphering host-pathogen dynamics.

Purpose of the Study:

To investigate the specific roles of HRs in host-pathogen interactions (HPIs).
To characterize how different pathogen types (eukaryotic, prokaryotic, viral) engage with human HRPs.
To introduce a resource for studying HRPs and HRs in HPIs.

Main Methods:

Comparative analysis of HRP and HR usage by eukaryotic, prokaryotic, and viral pathogens.
Characterization of HR types (sparse, abundant, polar, non-polar) engaged by pathogens.
Development and presentation of the Hi-PHI database.

Main Results:

Pathogens engage physiologically important human HRPs, influencing host processes.
Eukaryotic pathogens use host-sparse HRs for discriminate interactions.
Prokaryotic pathogens utilize host-abundant non-polar HRs via proxies for varied interactions.
Viral pathogens employ host-abundant polar uncharged HRs for promiscuous interactions through mimicry.

Conclusions:

Pathogen strategies for engaging human HRPs vary based on pathogen type and HR characteristics.
The Hi-PHI resource facilitates further research into HRPs and HRs in HPIs.
Potential therapeutic strategies include repurposing drugs targeting engaged HRPs and developing anti-infectives targeting HRs.