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Dimeric Collection

"Dimeric: Unveiling the Intricate World of Protein Interactions" Proteins are the building blocks of life

Background imageDimeric Collection: Immunoglobulin A, molecular model

Immunoglobulin A, molecular model
Immunoglobulin A. Molecular model of the structure of the antibody immunoglobulin A (IgA). This is the secretory dimeric form (sIgA), the main immunoglobulin found in secretions such as saliva

Background imageDimeric Collection: Epstein-Barr virus protein bound to DNA C014 / 0875

Epstein-Barr virus protein bound to DNA C014 / 0875
Epstein-Barr virus protein bound to DNA. Computer model showing a molecule of Epstein-Barr nuclear antigen 1 (EBNA1) bound to a strand of DNA (deoxyribonucleic acid)

Background imageDimeric Collection: H-NS chromatin-structuring protein

H-NS chromatin-structuring protein. Molecular model of the oligomerization domain of the H-NS protein from the Escherichia coli bacterium. This dimeric molecule folds in on itself, as shown here

Background imageDimeric Collection: Newcastle disease virus protein C015 / 6912

Newcastle disease virus protein C015 / 6912
Newcastle disease virus protein, molecular model. This is a hemagglutinin-neuromidase (HN) protein that enables the virus to bind to and infect host cells

Background imageDimeric Collection: Kinesin motor protein dimer C015 / 5921

Kinesin motor protein dimer C015 / 5921
Kinesin motor protein dimer, molecular model. Kinesin is a motor protein that moves along microtubule filaments in cells. It does so by forming a dimer, the heads of which walk along the microtubule

Background imageDimeric Collection: Kinesin motor protein dimer C015 / 5920

Kinesin motor protein dimer C015 / 5920
Kinesin motor protein dimer, molecular model. Kinesin is a motor protein that moves along microtubule filaments in cells. It does so by forming a dimer, the heads of which walk along the microtubule

Background imageDimeric Collection: SMAD4 protein domain bound to DNA C015 / 6552

SMAD4 protein domain bound to DNA C015 / 6552
SMAD4 protein domain bound to DNA, molecular model. This strand of DNA (deoxyribonucleic acid, green and pink) is surrounded by MH1 domains of the SMAD4 (Mothers against decapentaplegic homolog 4)

Background imageDimeric Collection: SMAD4 protein domain bound to DNA C015 / 6551

SMAD4 protein domain bound to DNA C015 / 6551
SMAD4 protein domain bound to DNA, molecular model. This strand of DNA (deoxyribonucleic acid, red and blue) is surrounded by MH1 domains of the SMAD4 (Mothers against decapentaplegic homolog 4)

Background imageDimeric Collection: Interferon antagonism by viral protein C015 / 5421

Interferon antagonism by viral protein C015 / 5421
Interferon (IFN) antagonism by viral protein. Molecular model of an orthopoxvirus IFN-gamma-binding protein tetramer bound to an IFN-gamma dimer

Background imageDimeric Collection: Interferon antagonism by viral protein C015 / 5420

Interferon antagonism by viral protein C015 / 5420
Interferon (IFN) antagonism by viral protein. Molecular model of an orthopoxvirus IFN-gamma-binding protein tetramer bound to an IFN-gamma dimer

Background imageDimeric Collection: Lysyl oxidase enzyme molecule

Lysyl oxidase enzyme molecule. Computer artwork showing the secondary structure of the enzyme lysyl oxidase (LOX). LOX is a homodimeric (composed of two identical subunits)



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"Dimeric: Unveiling the Intricate World of Protein Interactions" Proteins are the building blocks of life, and their interactions play a crucial role in various biological processes. Among these interactions, dimerization stands out as a fascinating phenomenon that brings together two protein subunits to form a functional unit. In this captivating journey into the world of dimers, we explore some intriguing examples. Firstly, we encounter the Epstein-Barr virus protein bound to DNA C014/0875. This dimeric complex plays a pivotal role in viral replication and pathogenesis by manipulating host cell machinery. Moving on, our exploration takes us to Immunoglobulin A's molecular model—a remarkable example of dimerization in antibody structure. This process enhances its ability to neutralize pathogens and protect our immune system. Next up is the H-NS chromatin-structuring protein—an essential player in organizing bacterial DNA. Its dimeric form ensures proper gene regulation and genome stability. Continuing our expedition through diverse proteins, we stumble upon Newcastle disease virus protein C015/6912—a striking example of viral hijacking mechanisms involving dimer formation for efficient infection. The Kinesin motor protein dimers C015/5921 and C015/5920 captivate us with their role in intracellular transport along microtubules—essential for cellular functioning and division. Our journey then leads us to SMAD4 protein domains bound to DNA C015/6552 and C015/6551—key players in TGF-beta signaling pathway regulation. These dimers orchestrate intricate cellular responses critical for development and homeostasis. As we delve deeper into viral strategies, interferon antagonism by viral proteins C015/5421 and C015/5420 emerges as an intriguing mechanism employed by viruses to evade host immune defenses through disrupting antiviral responses mediated by interferons.