High impact information on NRP1

• Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M domain [1].
• In solution at acid pH, the glutamine-rich and asparagine-rich 18-residue Sup35 peptide, rendered soluble by the addition of two aspartates at the amino end and two lysines at the carboxyl end, gives a beta-sheet CD spectrum; it aggregates at neutral pH [2].
• The C-terminal domain of Ure2p controls nitrogen catabolism by complexing with the transcription factor, Gln3p, whereas the asparagine-rich N-terminal "prion" domain is responsible for amyloid filament formation (prion conversion) [3].
• The gene for PUB1 was cloned and sequenced, and the sequence was found to predict a 51-kDa protein with three ribonucleoprotein consensus RNA-binding domains and three glutamine- and asparagine-rich auxiliary domains [4].
• Therefore the genes are proposed to be named AZF1 (asparagine-rich zinc-finger protein) and PGD1 (polyglutamine domain protein) [5].

Associations of NRP1 with chemical compounds

• A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions [6].
• The second ORF is asparagine-rich and very serine-rich, with a remarkable stretch of nearly 26 consecutive asparagine residues comprised of the same codon [7].

Other interactions of NRP1

• These characteristic structural features were used to create the abbreviation AZF1 (Asparagine-rich Zinc Finger protein) [8].

References