Final answer:
The large multiprotein assembly at the nuclear pore is called the Nuclear Pore Complex, which regulates the movement of molecules between the nucleus and the cytoplasm.
Step-by-step explanation:
The large multiprotein assembly at the nuclear pore is known as the Nuclear Pore Complex (NPC). The nuclear envelope, which is a double membrane, encloses the nucleus and contains these nuclear pores.
These nuclear pores are critical for controlling the movement of molecules between the nucleus and the cytoplasm.
They are lined with proteins that regulate this passage, allowing large molecules like proteins and RNA to move in and out of the nucleus, which is essential for processes such as protein synthesis and the maintenance of genetic material.
The nuclear pore complex predominantly consists of proteins known as nucleoporins, with each NPC comprising at least 456 individual protein molecules, and 34 distinct nucleoporin proteins.
About half of the nucleoporins encompass solenoid protein domains, such as alpha solenoids or beta-propeller folds, and occasionally both as separate structural domains.
Conversely, the remaining nucleoporins exhibit characteristics of "natively unfolded" or intrinsically disordered proteins, characterized by high flexibility that lack ordered tertiary structure.
These disordered proteins, referred to as FG nucleoporins, contain multiple phenylalanine–glycine repeats (FG repeats) in their amino acid sequences.