es have pictures of structural features of BA Use them to answer ne HIV protease
ID: 179268 • Letter: E
Question
es have pictures of structural features of BA Use them to answer ne HIV protease, BACE1 an enzyme with two aspartates at its the questions below. Like BACE1 a membra bound protease. active site, and it a "flap". (A) Describe in the secondary structural and other features that you observe in BACE1's tertiary structure. (B) Where is the catalytic domain located in (or on) the cell? (C) The most likely structural arrangement of the transmembrane domain sequence is as a single strand of a-heli How thick does the cell membrane seem to be? particularly important parts of the catalytic chain and an conformation changes that occur during the action of the enzyme (binding of substrate and proteolysis) (E) How do the two aspartates function in the catalytic activity of the enzyme? (F) The authors of the J Neurosci article s that the inhibitor BTDN probably binds to the membrane domain. What kind of forces might be involved in that binding interaction? Look at BTDN' structure and the amino acid side chains that are present and take into consideration the structure of the a-helix when devising your answer. are the structures/characteristics of BACE1 and HIV protease (see pictures (G) below).Explanation / Answer
BACE1 is confined to neurons and is essential for peripheral nerve myelination and axonal bundling of schwann cells.
The enzyme is a 456 residue protein with a N terminal or extracellular region with 412 residues where 2 aspartyl acid residues act as active sites and 23 residue C terminal and 21 residue transmembrane region.
Secondary structure shows the alpha helices, beta sheets and ramdom coil. There are no significant structural difference between active and inactive forms. Inactive form is more stable structurally.
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