Protein Name: Histone chaperone RbAp46
Title of Drawing: “Cologne Fools’ Guild”
Protein Data Bank ID: 3CFS
This protein helps to organize histones, the spools around which DNA is wrapped, and regulates genes involved in cell growth and transition.
Here, RbAp46 has undergone its own transition – a carnivalistic one. And voilà – welcome the Cologne Fools’ Guild! Cologne is one of the key cities for carnival celebrations, and today is Rosenmontag – the peak of the festivities with grand parades and costumes. It takes me right back to the fun Carnival days of my childhood in Cologne.
This drawing was inspired by a request by Ian Le Guillou long ago.
Protein Name: ErbB4 (extracellular domain)
Title of Drawing: “A Crab at Rest”
Protein Data Bank ID: 2AHX
The receptor tyrosine kinase ErbB4 is like a multi-module signal hub, consisting of a receptor and an enzyme. The receptor part receives signals, while the enzyme part sparks action inside the cell.
Imagine the receptor part as a hardworking crab perched on the surface of a cell.
The whole crab represents the receptor parts of two ErbB4 proteins. Its “arms” reach out to catch specific activating molecules called ligands. When the crab catches its “prey,” it stamps on the sea ground. These stamps send signals below the surface to creatures like clams (representing the intracellular enzyme part, not shown here). The clams snap their shells shut, passing messages further underground to other residents, much like a kinase enzyme triggers signaling cascades inside the cell.
When ErbB4 functions correctly, it supports growth and differentiation in tissues like the mammary gland and nervous system. However, if ErbB4 gets mutated, it might misfire, contributing to cancer. Interestingly, the word “cancer” comes from the Latin for “crab” because some tumors resemble crabs with their radiating “legs.”
In the drawing, the crab is shown playing with bubbles instead of catching prey, reflecting ErbB4 in its inactive state. When the time comes, this crab will switch from resting to working, catching its ligand and triggering vital cellular messages. But for now, it’s just a crab at rest.
Protein Data Bank ID: 1URN
Protein Name: Spliceosomal protein (snRNP U1A)
complexed with part of the spliceosomal RNA (snRNA U1)
Organism: Homo sapiens
Title of Drawing: “Paving the Way”
Proteins in our body are built based on instructions in our DNA. First, this code is transcribed into RNA. However, the initial RNA (pre-RNA) contains unwanted sections called introns that must be removed. This is where the spliceosome — a crew of protein actors (snRNPs) and RNA devices (snRNAs) — steps in. Imagine the intron as a tree blocking the path. The snRNP U1A, shown as a kangaroo, guides the U1 snRNA, depicted as a sledge, to the right spot on the pre-RNA. The sledge stops at the tree (intron), where the spliceosome crew cuts it down, clearing and splicing the path for the protein-making team to proceed.
Protein Data Bank ID: 1SGZ
Protein Name: BACE1/Beta-Secretase 1 (catalytic domain)
Organism: Homo sapiens
Title of Drawing: “Worn out sack of memories”
Alzheimer’s disease is a progressive brain disorder that slowly destroys memory, thinking skills, and the ability to carry out simple tasks. Age is the greatest risk factor, with approximately 5% of people aged 65–74 affected, and the probability rising to 13% for those in their next decade of life. This is a staggering figure, considering that it can strike anyone.
One of the key mysteries of Alzheimer’s disease is the abnormal processing of a protein called amyloid β precursor protein (APP). BACE1, the protein featured in this drawing, is an enzyme that acts like molecular scissors, cutting APP in a way that contributes to the disease. People with the most common form of late-onset Alzheimer’s often show elevated levels of BACE1.
To highlight BACE1’s role in this disease, the enzyme is portrayed as an old man holding a leaky sack, with memories dripping away, capturing the heartbreaking loss of memory associated with Alzheimer’s.
Protein Data Bank ID: 1AOI
Structure Name: Nucleosome
Organism: Xenopus laevis
Title of Drawing: “Atomic rat”
Nucleosomes are DNA packaging complexes that consist of eight histone proteins and a DNA segment wrapped around them, resembling thread wound around a spool. This drawing is based on two H3 and two H2B histone chains and a DNA stretch, with the long tail of H3 becoming the long tail of a rat.
The drawing is entitled “Atomic Rat” – a distant allusion to the comic strip superhero “Atomic Mouse” popular in the sixties. In analogy to the histones that are centerpieces holding DNA together, atoms are the units that bind “the world’s innermost core together” (Goethe, Faust I).
For the general public, proteins are just nutrients, like fats, carbohydrates, or other delicious foods. They are often associated with nothing more than eggs or muscle-building shakes. While not entirely wrong, as protein shakes and eggs indeed consist of proteins, this view is rather limited. Thinking of proteins only as food is as simplistic as seeing humans solely as eating machines.
Let’s take a closer look at what we’re actually consuming. A protein molecule can be imagined as a colorful bead necklace, with each bead representing an amino acid linked to others by a thread. During digestion, this necklace is broken into individual beads.
Surprisingly, our bodies aren’t fussy about the type of necklaces we eat. What matters is that they contain eight essential amino acids that we can’t produce ourselves. The remaining 12-13 amino acids are useful too, but if needed, our bodies can synthesize them. These beads are then reassembled into new necklaces based on a precise instruction dictated by our DNA. Humans produce hundreds of thousands of different necklaces, each serving a unique purpose.
Here’s where it gets exciting: the freshly assembled necklaces don’t stay flat. They immediately fold into complex three-dimensional structures. Each bead acts like a magnet, attracting or repelling others depending on its charge. This folding determines the protein’s function — much like we use different tools for different tasks: sharp ones for cutting, needle-shaped for piercing, and hollow for scooping.
Our protein toolbox is incredibly diverse. Some proteins act as tiny scissors, while others provide structural support, holding cells together like a frame. Some function as messengers or couriers. Others spin like hamsters in a wheel to generate energy. There are even proteins with decorative roles — like keratin, the key protein in our hair. Often, proteins team up to form large complexes, creating pumps or even motors. Proteins truly are marvels of nature, and life without them unimaginable.
It’s these intricate, functional forms of proteins that fascinate scientists. Researchers go to great lengths to study these structures — crystallizing proteins for X-ray imaging, exposing them to magnetic fields, bombarding them with electrons, or employing advanced computational efforts to model their shapes. Obtaining each three-dimensional structure is a monumental undertaking. Honoring these human achievements through art is nothing less than deserved!
Protein Data Bank ID: 4LCE
Protein Name: C-terminal-binding protein 1 (CTBP1)/
Refeldin A (BFA)-induced ADP-ribosylated substrate (BARS)
Organism: Homo sapiens
Title of Drawing: “Snow leopards”
This drawing was initiated by a good friend who is working on the BARS protein and is enthusiastic about small and big cats. As in the Russian language the snow leopard is often termed “(snow) bars”, the protein structure inevitably resulted in this feline couple.
BARS is a multifunctional protein. In the nucleus, it can bind a specific DNA region and thereby regulate the transition from epithelial to mesenchymal type of tissue. In the cytosol, it plays a role in membrane fission, including fragmentation of the Golgi apparatus.
Protein Data Bank ID: 1AOX
Protein Name: Integrin α2β1 I domain
Organism: Homo sapiens
Title of Drawing: “Community”
Another request from 2012, sorry for the huge delay, najas!
This scene is based on the integrin α2β1 I domain. Integrins are transmembrane proteins establishing connections between adjacent cells or between cells and the extracellular space. Integrin α2β1 can bind collagen or laminin and thereby not only ensures adhesion between the cellular skeleton and the extracellular matrix, but also can serve as a signal receiver for the cell.
The name “integrin” originates from the fact that these molecules are integral membrane proteins. Analogously to integrins incorporated into the membrane, members of religious groups such as Amish and Mennonites outlined in this drawing are highly integrated within their communities. An example to this is the warmth that has been bestowed on the sad girl by the other community members.
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It’s been a long time since I’ve posted a protein. But finally I’m back to the proteins and back for you, starting to fulfill your protein requests! The following drawing is inspired by a comment by pensatorkjh back in 2012.
Protein Data Bank ID: 3BEP
Protein Name: DNA Clamp
Organism: Escherichia coli
Title of the Drawing: “Even-Toed Ungulates”
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The DNA clamp is one of the most important cellular tools for DNA replication. It encircles the DNA helix which is situated in the center of the drawing and represents an emblem of even-toed ungulates. The clamp itself is drawn as a circle dance performed by deer, sheep, gazelles, and boars. The clamp slides along the DNA and ensures that the polymerase, the actual DNA copying machine, remains attached to the DNA strands. The clamp has distant analogy to a horse collar necessary for the carriage to remain on track.
Protein Art 