Homodimer Collection

HIV-1 protease molecule
HIV-1 protease, molecular model. This enzyme, from HIV (human immunodeficiency virus), cleaves viral polyproteins into functional proteins that are essential for viral assembly and infectivity

EcoRV restriction enzyme molecule C014 / 2117
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (purple and blue) bound to a DNA molecule (deoxyribonucleic acid, pink and white)

EcoRV restriction enzyme molecule C014 / 2112
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (pink) bound to a cleaved section of DNA (deoxyribonucleic acid, yellow)

EcoRV restriction enzyme molecule C014 / 2114
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (white and gold) bound to a cleaved section of DNA (deoxyribonucleic acid, orange and yellow)

EcoRV restriction enzyme molecule C014 / 2116
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (purple and blue) bound to a DNA molecule (deoxyribonucleic acid, pink and white)

EcoRV restriction enzyme molecule C014 / 2115
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (purple and blue) bound to a DNA molecule (deoxyribonucleic acid, pink and white)

EcoRV restriction enzyme molecule F006 / 9496
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (pink and yellow) bound to a cleaved section of DNA (deoxyribonucleic acid, red and blue)

EcoRV restriction enzyme molecule C014 / 2113
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (pink and blue) bound to a cleaved section of DNA (deoxyribonucleic acid, white)

EcoRV restriction enzyme molecule C014 / 2111
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (pink) bound to a cleaved section of DNA (deoxyribonucleic acid, grey)

EcoRV restriction enzyme molecule C014 / 2118
EcoRV restriction enzyme. Molecular model of the type II restriction enzyme EcoRV (purple and beige) bound to a DNA molecule (deoxyribonucleic acid, yellow and orange)

Stilbene synthase molecule C014 / 2292
Stilbene synthase, molecular model. This enzyme is produced by some plants (including grapes, peanuts and blueberries) in response to stress from either ultraviolet light or certain fungi

Stilbene synthase molecule C014 / 2291
Stilbene synthase, molecular model. This enzyme is produced by some plants (including grapes, peanuts and blueberries) in response to stress from either ultraviolet light or certain fungi

UVR8 protein molecule C014 / 4913
UVR8 protein molecule. Computer model showing photoreception of UV-B (ultraviolet-B) light rays (white beam, left) by a UVR8 protein, whose secondary structure (purple ribbons) is shown

UVR8 protein molecule C014 / 4912
UVR8 protein molecule. Computer model showing photoreception of UV-B (ultraviolet-B) light rays (top) by a UVR8 protein. The secondary structure (purple ribbons) of UVR8 is shown at bottom

DNA transcription control. Computer model showing a molecule of the FP50 homodimer (green) from NF-kB (nuclear factor kappa-light-chain-enhancer of activated B cells)

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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A homodimer is a fascinating molecular structure that plays a crucial role in various biological processes. One such example is the HIV-1 protease molecule, which forms a homodimer to carry out its vital function of cleaving viral polyproteins during replication. This dimeric arrangement allows for efficient and precise processing of these proteins, ultimately contributing to the maturation of infectious viral particles. Similarly, the EcoRV restriction enzyme molecule also exists as a homodimer. This enzyme acts as a defense mechanism in bacteria by recognizing specific DNA sequences and cutting them at precise locations. The dimeric form enhances its efficiency in target recognition and catalytic activity, ensuring accurate DNA cleavage. Within this family of EcoRV restriction enzymes, different variants like C014/2117, C014/2112, C014/2114, C014/2116, C014/2115, and F006/9496 have been identified. Each variant possesses distinct properties due to slight differences in their amino acid sequences or structural arrangements within the homodimeric complex. Moreover, scientists have extensively studied the interaction between HIV-1 protease molecules and inhibitors to develop effective antiviral drugs. By understanding how these inhibitors bind to each monomer within the homodimeric structure of HIV-1 protease molecules, researchers can design compounds that disrupt their enzymatic activity and hinder viral replication. In summary, whether it be through facilitating viral maturation or safeguarding bacterial genomes from foreign DNA invasion; homodimers like those formed by HIV-1 protease molecules or EcoRV restriction enzymes play critical roles in maintaining cellular integrity. Exploring their structures and functions not only deepens our knowledge of molecular biology but also paves the way for innovative therapeutic strategies against diseases caused by viruses or genetic abnormalities.