Nuclear pores are large
protein complexes that cross the
nuclear envelope, which is the double
membrane surrounding the
eukaryotic cell nucleus. There are about on average 2000 nuclear pore complexes in the
nuclear envelope of a vertebrate cell, but it varies depending on the number of transcriptions of the cell. The proteins that make up the nuclear pore complex are known as nucleoporins. About half of the nucleoporins typically contain either an
alpha solenoid or a
beta-propeller fold, or in some cases both as separate
structural domains. The other half exhibit structural characteristics typical of "natively unfolded" proteins, i.e. they are highly flexible proteins that lack ordered secondary structure. These disordered proteins are the FG nucleoporins, so called because their amino-acid sequence contains many repeats of the peptide
phenylalanine—
glycine.
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