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Protein–DNA interactions occur when a protein binds a molecule of DNA, often to regulate the biological function of DNA, usually the expression of a gene. Among the proteins that bind to DNA are transcription factors that activate or repress gene expression by binding to DNA motifs and histones that form part of the structure of DNA and bind ...
n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is a uniporter protein that in humans is encoded by the SLC2A1 gene. GLUT1 facilitates the transport of glucose across ...
Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. [2] Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6]
It is responsible for the low level of basal glucose uptake required to sustain respiration in all cells. Levels in cell membranes are increased by reduced glucose levels and decreased by increased glucose levels. GLUT1 expression is upregulated in many tumors. GLUT2: Is a bidirectional transporter, allowing glucose to flow in 2 directions.
Glucose transporters are classified into three groups based on sequence similarity, with a total of 14 members.All GLUT proteins share a common structure: 12 transmembrane segments, a single N-linked glycosylation site, a large central cytoplasmic linker, and both N- and C-termini located in the cytoplasm. [4]
The term DNA glycation applies to DNA damage induced by reactive carbonyls (principally methylglyoxal and glyoxal) that are present in cells as by-products of sugar metabolism. [13] Glycation of DNA can cause mutation, breaks in DNA and cytotoxicity. [13] Guanine in DNA is the base most susceptible to glycation. Glycated DNA, as a form of ...
The C-terminal tetramerization helix is not shown. The repressor is shown in complex with operator DNA (gold) and ONPF (green), an anti-inducer ligand (i.e. a stabilizer of DNA binding) The lac repressor (LacI) is a DNA-binding protein that inhibits the expression of genes coding for proteins involved in the metabolism of lactose in bacteria.
DNA glycosylases catalyze the first step of this process. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. This is accomplished by flipping the damaged base out of the double helix followed by cleavage of the N-glycosidic bond. [1]