Muscarinic acetylcholine receptors are G protein-coupled receptor complexes in the cell membranes of certain neurons and cells. They play several roles, including acting as the main end-receptor stimulated by acetylcholine released from postganglionic fibers in the parasympathetic nervous system. This 3D printed protein model of muscarinic acetylcholine receptor is visualized by its ribbon structure highlighting the protein’s transmembrane active sites.
This is a 3D print of RsmE bound to two strands of mRNA visualized as a ribbon bound to nucleotide sequences. The RsmE homodimer is colored blue and purple according to protein’s beta sheet and helices. In red and orange are the two RNA-binding sites. mRNA is colored shades of green according to nucleotide type.
Use this 3D printed Biologic Model of Tresiba Insulin Hexamer as a desktop reminder to take your medication before each meal.
Use this 3D printed Biologic Model of Novolog Insulin Hexamer as a desktop reminder to take your medication before each meal.
Trypsin is a protease enzyme from the digestive system. Trypsin hydrolyzes proteins adding water molecules to specific structures and cuts up other proteins into pieces. Trypsin is used in a variety of biotechnologies to break down proteins, commonly referred to as trypsinization.
“An understanding of the physiological and toxicological properties of borate and the utilization of boronic acids in drug development require a basic understanding of borate-enzyme chemistry. We report here the extension of our recent NMR studies indicating the formation of a ternary borate-alcohol-trypsin complex. Crystallographic and solution state NMR studies of porcine trypsin were performed in the presence of borate and either of three alcohols designed to bind to the S1 affinity subsite: 4-aminobutanol, guanidine-3-propanol, and 4-hydroxymethylbenzamidine. Quaternary complexes of trypsin, borate, S1-binding alcohol, and ethylene glycol (a cryoprotectant), as well as a ternary trypsin, borate, and ethylene glycol complex have been observed in the crystalline state. Borate forms ester bonds to Ser195, ethylene glycol (two bonds), and the S1-binding alcohol (if present). Spectra from (1)H and (11)B NMR studies confirm that these complexes also exist in solution and also provide evidence for the formation of ternary trypsin, borate, and S1-subsite alcohol complexes which are not observed in the crystals using our experimental protocols. Analysis of eight crystal structures indicates that formation of an active site borate complex is in all cases accompanied by a significant (approximately 4%) increase in the b-axis dimension of the unit cell. Presumably, our inability to observe the ternary complexes in the crystalline state arises from the lower stability of these complexes and consequent inability to overcome the constraints imposed by the lattice contacts. A mechanism for the coupling of the lattice contacts with the active site that involves a conformational rearrangement of Gln192 is suggested. The structures presented here represent the first crystallographic demonstration of covalent binding of an enzyme by borate.” ~RCSB
PDB ID: 1S81
This 3D printed model of Porcine Trypsin is pritned in full-color sandstone and colored by the protein’s bFactor.